By0050-58L Manual [PDF]
ENTER SITE »»» DOWNLOAD PDF
CLICK HERE »»» BOOK READER
| Status: AVAILABLE |
Last checked: 8 Minutes ago!
In order to read or download By0050-58L Manual [PDF] ebook, you need to create a FREE account.
| Download Now! |
eBook includes PDF, ePub and Kindle version
| ✔ Register a free 1 month Trial Account. |
| ✔ Download as many books as you like (Personal use) |
| ✔ Cancel the membership at any time if not satisfied. |
| ✔ Join Over 80000 Happy Readers |
By0050-58L Manual [PDF]
The first 4 characters of the case number is the movement number. By continuing to browse our website you accept the use of such cookies.For our privacy policy. Create one here. Before use, please read this instruction manual. Whether you are looking to get a quality workout in while the weather bad, or you are just looking to do a little warm 106 Problems and Solutions manual for fl23r electric fireplace master 2308. SLH4422MWCN Sunbeam Low Profile Heater with Manual Controls SLH4422MWCN User Manual.Despite popular belief they can be effective and they can get the job done. Check out our guide. Red abierta arris54g manual. Nov 05, 2015 Metodo de Wifi Red Abierta Al Ingresar Al Navegador Diego Condory. Loading Unsubscribe from Diego Condory? 31 Jul 2019 Saturn repair manuals online. Mind gym an athletes By0050 58l manual meat. Building internet V810c manual lymphatic drainage.Creators are allowed to post content they produce to the platform, so long as they comply with our policies. United Kingdom. Company number 10637289. User Agreement, Privacy, Cookies and AdChoice Norton Secured - powered by Verisign Amounts shown in italicised text are for items listed in currency other than Euros and are approximate conversions to Euros based upon Bloomberg's conversion rates. For more recent exchange rates, please use the Universal Currency Converter This page was last updated: 18-Aug 04:50. Number of bids and bid amounts may be slightly out of date. See each listing for international postage options and costs. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) Such methods entail administering A-beta fragments from a central or C-terminal regions of A-beta.
http://wekeepyoung.com/UserFiles/crestron-tpmc-4x-manual.xml
- Tags:
- by0050-58l manual.
Such fragments can induce a polyclonal mixture of antibodies that specifically bind to soluble A-beta without binding to plaques. The antibodies can inhibit formation of amyloid deposits of A-beta in the brain of a patient from soluble A? thus preventing or treating the disease. Fragment A-beta 15-24 and subfragments of 5-10 contiguous amino acids thereof are preferred immunogens due to their capacity to generate a high titer of antibodies. In both types of disease, the pathology is the same but the abnormalities tend to be more severe and widespread in cases beginning at an earlier age. The disease is characterized by at least two types of lesions in the brain, senile plaques and neurofibrillary tangles. Senile plaques are areas of disorganized neuropil up to 150 ?m across with extracellular amyloid deposits at the center visible by microscopic analysis of sections of brain tissue. Neurofibrillary tangles are intracellular deposits of microtubule associated tau protein consisting of two filaments twisted about each other in pairs. Nature 353, 844 (1991)) (valine 717 to glycine); Murrell et al., Science 254, 97 (1991) (valine 717 to phenylalanine); Mullan et al., Nature Genet. 1, 345 (1992) (a double mutation changing lysine 595 -methionine 596 to asparagine 595 -leucine 596 ). Such mutations are thought to cause Alzheimer's disease by increased or altered processing of APP to A?, particularly processing of APP to increased amounts of the long form of A? (i.e., A?1-42 and A?1-43). Mutations in other genes, such as the presenilin genes, PS1 and PS2, are thought indirectly to affect processing of APP to generate increased amounts of long form A? (see Hardy, TINS 20, 154 (1997)). These observations indicate that A?, and particularly its long form, is a causative element in Alzheimer's disease.
http://navigator-nsk.ru/userfiles/crestron-tpmc-8x-ga-manual.xml
Also, a strong correlation has been reported between antibodies that were efficacious in vivo and in an ex vivo assay using sections of PDAPP or Alzheimer's disease (AD) brain to measure plaque clearing activity. Fc receptors on microglial cells effected the clearance response in the ex vivo assay. Short-term treatment with this antibody has also been reported to improve performance in an object recognition task without affecting amyloid burden (Dodart et al., (2002) Nat. Neurosci., 5, 452-457). Sera from all animals immunized with A?15-24 were able to capture soluble A?1-42 (one serum sample had a titer higher than 1:1,350 and a precise titer was not determined), compared with 27 of those in the A?1-5 group and 3 of the A?3-9 group. FIGS. 2 B-C. Amyloid burden (FIG. 2B) and neuritic pathology (FIG. 2C) were evaluated with image analysis by a blinded microscopist. Values are expressed as a percentage of the mean of the A?5-1 group (negative control reversemer peptide). The A?5-11 group was evaluated at a separate sitting from the other groups, but in conjunction with the same negative control group as an internal reference (second A?5-1 reversemer set, on the left). Amyloid burden was significantly reduced in the A?-5, A?3-9, and A?5-11 groups (p The antibodies can inhibit formation of amyloid deposits of A? in the brain of a patient from soluble A?, thus preventing or treating the disease.Conservative substitutions involve substitutions between amino acids in the same class.Typically, fragments compete with the intact antibody from which they were derived for specific binding to an antigen fragment including separate heavy chains, light chains Fab, Fab. F(ab?)2, Fabc, and Fv. Fragments are produced by recombinant DNA techniques, or by enzymatic or chemical separation of intact immunoglobulins. The term “antibody” also includes one or more immunoglobulin chains that are chemically conjugated to, or expressed as, fusion proteins with other proteins.
http://www.raumboerse-luzern.ch/mieten/elfa-ds8000-1-dishwasher-manual
The term “antibody” also includes bispecific antibody. A? has several natural occurring forms. The natural human forms of A? are referred to as A?39, A?40, A?41, A?42 and A?43. The sequences of these peptides and their relationship to the APP precursor are illustrated by FIG. 1 of Hardy et al., TINS 20, 155-158 (1997). For example, A?42 has the sequence: See Kang et al., Nature, 325, 773 (1987); Ponte et al., Nature, 331, 525 (1988); and Kitaguchi et al., Nature, 331, 530 (1988). Amino acids within the human amyloid precursor protein (APP) are assigned numbers according to the sequence of the APP770 isoform. Terms such as A?39, A?40, A?41, A?42 and A?43 refer to an A? peptide containing amino acid residues 1-39, 1-40, 1-41, 1-42 and 1-43, respectively. Disaggregated A? or fragments thereof are generally soluble, and are capable of self-aggregating to form soluble oligomers. Oligomers of A? and fragments thereof are usually soluble and exist predominantly as alpha-helices or random coils. One method to prepare monomeric A? is to dissolve lyophilized peptide in neat DMSO with sonication. The resulting solution is centrifuged to remove any insoluble particulates. Aggregated A? or fragments thereof, means oligomers of A? or immunogenic fragments thereof in which the monomeric units are held together by noncovalent bonds and associate into insoluble beta-sheet assemblies. Aggregated A? or fragments thereof, means also means fibrillar polymers. Fibrils are usually insoluble. Some antibodies bind either soluble A? or fragments thereof or aggregated A? or fragments thereof. Some antibodies bind both soluble A? or fragments thereof and aggregated A? or fragments thereof. B-cell epitopes can be formed both from contiguous amino acids or noncontiguous amino acids juxtaposed by tertiary folding of a protein.
http://heidelberg-schloss.com/images/canon-visualizer-re-350-manual.pdf
Epitopes formed from contiguous amino acids are typically retained on exposure to denaturing solvents whereas epitopes formed by tertiary folding are typically lost on treatment with denaturing solvents. An epitope typically includes at least 3, and more usually, at least 5 or 8-10 amino acids in a unique spatial conformation. T-cells recognize continuous epitopes of about nine amino acids for CD8 cells or about 13-15 amino acids for CD4 cells. T cells that recognize the epitope can be identified by in vitro assays that measure antigen-dependent proliferation, as determined by 3 H-thymidine incorporation by primed T cells in response to an epitope (Burke et al., J. Inf. Dis., 170, 1110-19 (1994)), by antigen-dependent killing (cytotoxic T lymphocyte assay, Tigges et al., J. Immunol., 156, 3901-3910) or by cytokine secretion. Such a response can be an active response induced by administration of immunogen or a passive response induced by administration of antibody or primed T-cells. The response may also involve activation of monocytes, macrophages, NK cells, basophils, dendritic cells, astrocytes, microglia cells, eosinophils or other components of innate immunity. The relative contributions of humoral and cellular responses to the protective or therapeutic effect of an immunogen can be distinguished by separately isolating antibodies and T-cells from an immunized syngeneic animal and measuring protective or therapeutic effect in a second subject. Competitive inhibition is measured by determining the amount of label bound to the solid surface or cells in the presence of the test immunoglobulin. Usually the test immunoglobulin is present in excess. Antibodies identified by competition assay (competing antibodies) include antibodies binding to the same epitope as the reference antibody and antibodies binding to an adjacent epitope sufficiently proximal to the epitope bound by the reference antibody for steric hindrance to occur.
Usually, when a competing antibody is present in excess, it will inhibit specific binding of a reference antibody to a common antigen by at least 50 or 75. The fluorescence intensity of antibodies that bind to soluble A? peptide without binding to plaques is within a factor of five, sometimes within a factor of two and sometimes indistinguishable within experimental error from that of the control antibody. Generally, T-cell epitopes are greater than 10 contiguous amino acids. Therefore, preferred fragments of A? are of size 5-10 or preferably 7-10 contiguous amino acids; i.e., sufficient length to generate an antibody response without generating a T-cell response. Most T-cell epitopes occur within amino acids 14-30 of A?. These fragments can generate an antibody response that includes end-specific antibodies.In general, such fragments induce antibodies that specifically bind to and induce clearing of amyloid plaques via phagocytic cells. Such a response is particularly useful to clear existing deposits of A?. However, once the deposits have been cleared, further treatment with a fragment from the central or C-terminal region of A? to induce antibodies to soluble A? is advantageous for preventing further deposition of A? without risk of inflammatory side effects in certain patients. N-terminal fragments beginning at residues 1-3 of A? and ending at residues 7-11 of A? are particularly preferred.Analogs of A? induce antibodies that specifically bind with a natural A? peptide (e.g., A?42). Analogs of A? typically differ from naturally occurring peptides at up to 30 of amino acid positions by up to 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 position changes. Each deletion or substitution of a natural amino acid residue is considered a position change as is the insertion of a residue without substitution.Analogs of A? fragments induce antibodies that specifically bind with a natural A? peptide (e.g., A?42). Analogs of A?
fragments typically differ from naturally occurring peptide fragment at up to about 30 of amino acid positions. For example, an analog of A?15-21 may vary by up to 1, 2, 3 or 4 10 position changes. Each deletion or substitution of a natural amino acid residue is considered a position change as is the insertion of a residue without substitution.Some therapeutic agents of the invention are all-D peptides, e.g., all-D A? or all-D A? fragment, and all-D peptide analogs.Automatic peptide synthesizers are commercially available from numerous suppliers, such as Applied Biosystems, Foster City, Calif. Procedures for recombinant expression are described by Sambrook et al., Molecular Cloning: A Laboratory Manual (C.S.H.P. Press, NY 2d ed., 1989). Some forms of A? peptide are also available commercially (e.g., American Peptides Company, Inc., Sunnyvale, Calif. and California Peptide Research, Inc. Napa, Calif.). For example, preferred agents include fusion proteins comprising a segment of A? fused to a heterologous amino acid sequence that induces a helper T-cell response against the heterologous amino acid sequence and thereby a B-cell response against the A? segment. One or more flanking heterologous amino acids can also be used to cap an A? peptide to protect it from degradation in manufacture, storage or use. Such polypeptides can be screened for prophylactic or therapeutic efficacy in animal models in comparison with untreated or placebo controls as described below. Therapeutic agents of the invention include an immunogenic fragment of A? flanked by polylysine sequences.A nucleic acid encoding the immunogenic peptide is incorporated into a genome or episome of the virus or bacteria. Optionally, the nucleic acid is incorporated in such a manner that the immunogenic peptide is expressed as a secreted protein or as a fusion protein with an outer surface protein of a virus or a transmembrane protein of a bacteria so that the peptide is displayed.
Viruses or bacteria used in such methods should be nonpathogenic or attenuated. Suitable viruses include adenovirus, HSV, Venezuelan equine encephalitis virus and other alpha viruses, vesicular stomatitis virus, and other rhabdo viruses, vaccinia and fowl pox. Fusion of an immunogenic peptide to HBsAg of HBV is particularly suitable. For example, any peptides and proteins forming ? -pleated sheets can be screened for suitability. Anti-idiotypic antibodies against monoclonal antibodies to A? or other amyloidogenic peptides can also be used.Combinatorial libraries can be produced for many types of compounds that can be synthesized in a step-by-step fashion. Such compounds include polypeptides, beta-turn mimetics, polysaccharides, phospholipids, hormones, prostaglandins, steroids, aromatic compounds, heterocyclic compounds, benzodiazepines, oligomeric N-substituted glycines and oligocarbamates.For example, initial screens can be performed with any polyclonal sera or monoclonal antibody to A? or a fragment thereof Compounds can then be screened for specifically binding to a specific epitope within A? (e.g., 15-24). Compounds can be tested by the same procedures described for mapping antibody epitope specificities. Compounds identified by such screens are then further analyzed for capacity to induce antibodies or reactive lymphocytes to A? or fragments thereof For example, multiple dilutions of sera can be tested on microtiter plates that have been precoated with A? or a fragment thereof and a standard ELISA can be performed to test for reactive antibodies to A? or the fragment. Compounds can then be tested for prophylactic and therapeutic efficacy in transgenic animals predisposed to an amyloidogenic disease, as described in the Examples. The same screening approach can be used on other potential agents analogs of A? and longer peptides including fragments of A?, described above.
In this situation, a peptide immunogen can be linked to a suitable carrier molecule to form a conjugate which helps elicit an immune response. A single agent can be linked to a single carrier, multiple copies of an agent can be linked to multiple copies of a carrier, which are in turn linked to each other, multiple copies of an agent can be linked to a single copy of a carrier, or a single copy of an agent can be linked to multiple copies of a carrier, or different carriers. T cell epitopes are also suitable carrier molecules. Immunogens may be linked to the carries with or with out spacers amino acids (e.g., gly-gly). Some T cell epitopes are promiscuous while other T cell epitopes are universal. Promiscuous T cell epitopes are capable of enhancing the induction of T cell immunity in a wide variety of subjects displaying various HLA types. Further examples include: A preferred PADRE peptide is AKXVAAWTLKAAA (SEQ ID NO:11), (common residues bolded) wherein X is preferably cyclohexylalanine tyrosine or phenylalanine, with cyclohexylalanine being most preferred. Techniques for linking an immunogen to a carrier include the formation of disulfide linkages using N-succinimidyl-3-(2-pyridyl-thio) propionate (SPDP) and succinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) (if the peptide lacks a sulfhydryl group, this can be provided by addition of a cysteine residue). These reagents create a disulfide linkage between themselves and peptide cysteine resides on one protein and an amide linkage through the epsilon-amino on a lysine, or other free amino group in other amino acids. Many of these thio-ether-forming agents are commercially available and include reactive esters of 6-maleimidocaproic acid, 2-bromoacetic acid, and 2-iodoacetic acid, 4-(N-maleimido-methyl)cyclohexane-1-carboxylic acid. The carboxyl groups can be activated by combining them with succinimide or 1-hydroxyl-2-nitro-4-sulfonic acid, sodium salt.
The conformational separation between the helper epitope and the antibody eliciting domain thus permits more efficient interactions between the presented immunogen and the appropriate T h and B cells. The mixture may contain a mixture of at least two conjugates with different T h cell epitopes, a mixture of at least three conjugates with different T h cell epitopes, or a mixture of at least four conjugates with different T h cell epitopes. The mixture may be administered with an adjuvant. The immunogenic peptide can be linked at its amino terminus, its carboxyl terminus, or both to a carrier. Optionally, multiple repeats of the immunogenic peptide can be present in the fusion protein. Optionally, an immunogenic peptide can be linked to multiple copies of a heterologous peptide, for example, at both the N and C termini of the peptide. Optionally, multiple copies of an immunogenic peptide can be linked to multiple copies of a heterologous peptide.Some carrier peptides serve to induce a helper T-cell response against the carrier peptide.Some of these fusion proteins comprise segments of A? linked to tetanus toxoid epitopes such as described in U.S. Pat. No. 5,196,512, EP 378,881 and EP 427,347. Some fusion proteins comprise segments of A? linked to at least one PADRE peptide described in U.S. Pat. No. 5,736,142. Some heterologous peptides are promiscuous T-cell epitopes, while other heterologous peptides are universal T-cell epitopes. In some methods, the agent for administration is simply a single fusion protein with an A? segment linked to a heterologous segment in linear configuration. The therapeutic agents of the invention can be represented using a formula. When x is two, such a multimer has four fusion proteins linked in a preferred configuration referred to as MAP4 (see U.S. Pat. No. 5,229,490). Depending upon the number of times lysine is incorporated into the sequence and allowed to branch, the resulting structure will present multiple N termini.
In this example, four identical N termini have been produced on the branched lysine-containing core. Such multiplicity greatly enhances the responsiveness of cognate B cells. In the examples below, Z refers to an immunogenic fragment of A?, and Z1-4 refer to immunogenic fragment(s) of A?. The fragments can be the same as each other or different. Such nucleic acids can be DNA or RNA. A nucleic acid segment encoding an immunogen is typically linked to regulatory elements, such as a promoter and enhancer, that allow expression of the DNA segment in the intended target cells of a patient. For expression in blood cells, as is desirable for induction of an immune response, promoter and enhancer elements from light or heavy chain immunoglobulin genes or the CMV major intermediate early promoter and enhancer are suitable to direct expression. The linked regulatory elements and coding sequences are often cloned into a vector. For administration of double-chain antibodies, the two chains can be cloned in the same or separate vectors. The nucleic acids encoding therapeutic agents of the invention can also encode at least one T cell epitope.Suitable lipids and related analogs are described by U.S. Pat. No. 5,208,036, 5,264,618, 5,279,833 and 5,283,185. The microprojectiles are accelerated with a shock wave or expanding helium gas, and penetrate tissues to a depth of several cell layers.A variety of adjuvants can be used in combination with an immunogenic fragment of A?, to elicit an immune response. Preferred adjuvants augment the intrinsic response to an immunogen without causing conformational changes in the immunogen that affect the qualitative form of the response. Adjuvants can be administered as a component of a therapeutic composition with an active agent or can be administered separately, before, concurrently with, or after administration of the therapeutic agent.
Such adjuvants can be used with or without other specific immunostimulating agents such as MPL or 3-DMP, QS-21, polymeric or monomeric amino acids such as polyglutamic acid or polylysine. Another class of adjuvants is oil-in-water emulsion formulations. Other adjuvants include RC-529, GM-CSF and Complete Freund's Adjuvant (CFA) and Incomplete Freund's Adjuvant (IFA).Immunogen and adjuvant can be packaged and supplied in the same vial or can be packaged in separate vials and mixed before use. Immunogen and adjuvant are typically packaged with a label indicating the intended therapeutic application. If immunogen and adjuvant are packaged separately, the packaging typically includes instructions for mixing before use. For example, Complete Freund's adjuvant is not suitable for human administration. Alum, MPL and QS-21 are preferred. Optionally, two or more different adjuvants can be used simultaneously. Preferred combinations include alum with MPL, alum with QS-21, MPL with QS-21, MPL or RC-529 with GM-CSF, and alum, QS-21 and MPL together.The antibodies used for passive administration can be antibodies to N-terminal epitopes of A? for induction of a phagocytic clearing response of plaques, or can be antibodies to central or C-terminal regions of A? for clearing soluble A?. In some methods, passive administration with an antibody to an N-terminal region antibody is performed first to clear existing amyloid deposits. When an antibody is said to specifically bind to an epitope within specified residues, such as A?1-5 for example, what is meant is that the antibody specifically binds to a polypeptide containing the specified residues (i.e., A?1-5 in this an example). Such an antibody does not necessarily contact every residue within A?1-5. Nor does every single amino acid substitution or deletion with in A?1-5 necessarily significantly affect binding affinity.
Several mouse antibodies of different binding specificities are available as starting materials for making humanized antibodies. Human isotype IgG1 is preferred for antibodies to the N-terminal region of because of it having highest affinity of human isotypes for the FcRI receptor on phagocytic cells. Some antibodies specifically bind to A? with a binding affinity greater than or equal to about 10 7, 10 8, 10 9, or 10 10 M ?1. Therefore, the present methods can be administered prophylactically to the general population without the need for any assessment of the risk of the subject patient. The present methods are especially useful for individuals who do have a known genetic risk of Alzheimer's disease. Such individuals include those having relatives who have experienced this disease, and those whose risk is determined by analysis of genetic or biochemical markers. Genetic markers of risk toward Alzheimer's disease include mutations in the APP gene, particularly mutations at position 717 and positions 670 and 671 referred to as the Hardy and Swedish mutations respectively (see Hardy, TINS, supra). Other markers of risk are mutations in the presenilin genes, PS1 and PS2, and ApoE4, family history of AD, hypercholesterolemia or atherosclerosis. Individuals presently suffering from Alzheimer's disease can be recognized from characteristic dementia, as well as the presence of risk factors described above. In addition, a number of diagnostic tests are available for identifying individuals who have AD. These include measurement of CSF tau and A?42 levels. Elevated tau and decreased A?42 levels signify the presence of AD.Treatment typically entails multiple dosages over a period of time. Treatment can be monitored by assaying antibody, or activated T-cell (a side effect) or B-cell responses to the therapeutic agent (e.g., A? peptide) over time. If the response falls, a booster dosage is indicated.
In some methods, administration of agent reduces or eliminates myocognitive impairment in patients that have not yet developed characteristic Alzheimer's pathology. An amount adequate to accomplish therapeutic or prophylactic treatment is defined as a therapeutically- or prophylactically-effective dose. A combination of amount and dosage frequency adequate to accomplish the therapeutic or prophylactic treatment is defined as a therapeutically- or prophylactically-effective regime. In both prophylactic and therapeutic regimes, agents are usually administered in several dosages until a sufficient immune response has been achieved. A dosage and frequency of administrations adequate to accomplish therapeutic or prophylactic treatment is defined as a therapeutically- or prophylactically-effective regime. Typically, the patieht's immune response is monitored and repeated dosages are given if the immune response starts to wane.Usually, the patient is a human but nonhuman mammals including transgenic mammals can also be treated. Treatment dosages need to be titrated to optimize safety and efficacy. The amount of immunogen depends on whether adjuvant is also administered, with higher dosages being required in the absence of adjuvant. The amount of an immunogen for administration sometimes varies from 1-500 ?g per patient and more usually from 5-500 ?g per injection for human administration. Occasionally, a higher dose of 1-2 mg per injection is used. Typically at least 10, 20, 50 or 100 ?g is used for each human injection. The mass of immunogen also depends on the mass ratio of immunogenic epitope within the immunogen to the mass of immunogen as a whole. The timing of injections can vary significantly from once a day, to once a year, to once a decade. A typical regimen consists of an immunization followed by booster injections at time intervals, such as 6 week intervals. Another regimen consists of an immunization followed by booster injections 1, 2 and 12 months later.
Another regimen entails an injection every two months for life. Alternatively, booster injections can be on an irregular basis as indicated by monitoring of immune response. An exemplary treatment regime entails administration once per every two weeks or once a month or once every 3 to 6 months. In some methods, two or more monoclonal antibodies with different binding specificities are administered simultaneously, in which case the dosage of each antibody administered falls within the ranges indicated. Antibody is usually administered on multiple occasions. Intervals between single dosages can be weekly, monthly or yearly. Dosage and frequency vary depending on the half-life of the antibody in the patient. In general, human antibodies show the longest half life, followed by humanized antibodies, chimeric antibodies, and nonhuman antibodies. The dosage and frequency of administration can vary depending on whether the treatment is prophylactic or therapeutic. In prophylactic applications, a relatively low dosage is administered at relatively infrequent intervals over a long period of time. Some patients continue to receive treatment for the rest of their lives. In therapeutic applications, a relatively high dosage at relatively short intervals is sometimes required until progression of the disease is reduced or terminated, and preferably until the patient shows partial or complete amelioration of symptoms of disease. The most typical route of administration of an immunogenic agent is subcutaneous although other routes can be equally effective. The next most common route is intramuscular injection. This type of injection is most typically performed in the arm or leg muscles. In some methods, agents are injected directly into a particular tissue where deposits have accumulated, e.g., intracranial injection. Intramuscular injection or intravenous infusion are preferred for administration of antibody (in combination therapies).
Add new comment