GM CSF (CSF2) Mouse Monoclonal Antibody [Clone ID: B-S37]

Specifications

Product Data
Clone Name	B-S37
Applications	ELISA
Recommend Dilution	ELISA.
Reactivity	Human
Host	Mouse
Clonality	Monoclonal
Immunogen	Recombinant Human GM-CSF.
Specificity	This antibody recognizes recombinant and natural GM-CSF (Granulocyte-macrophage colony-stimulating factor).
Formulation	Phosphate-buffered saline. Sterile-filtered through 0.22 µm. Carrier and preservative free. State: Azide Free State: Liquid purified IgG fraction Preservative: None
Concentration	lot specific
Purification	Ion Exchange Chromatography
Conjugation	Unconjugated
Storage Condition	Store the antibody undiluted at 2-8°C. DO NOT FREEZE!
Gene Name	colony stimulating factor 2
Database Link	Entrez Gene 1437 Human UniProt ID P04141
Background	Granulocyte-macrophage colony stimulating factor (GM-CSF) regulates hematopoiesis, cell migration and immunity. GM-CSF is crucial for the growth and development of granulocyte and macrophage progenitor cells particularly during host defence and inflammatory reactions. GM-CSF is glycosylated at two N-linked and several O-linked sites. Glycosylation of GMCSF is important as it can affect pharmacokinetics, receptor affinity, biological activity, in vivo clearance rates and immunoreactivity. Patients receiving human recombinant GM-CSF commonly develop antibodies that recognize recombinant human GM-CSF produced in yeast (sargramostim) and E. coli (molgramostin), which exhibit glycosylation patterns that are distinct to the native human glycosylation. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible.
Synonyms	CSF2, GMCSF, Sargramostim, Molgramostin
Reference Data

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