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Guinea pig anti-goat igg heavy chain polyclonal Antibody
Product Name Guinea pig anti-goat igg heavy chain polyclonal Antibody
Catalog Number CSB-PA00770E0Gp
Immunogen goat igg heavy chain
Raised in Guinea pig
Species Reactivity goat
Tested applications WB;ELISA
Application notes
Relevance The basic structure of IgG molecule is composed of four polypeptide chains, that is, from the same two small molecular weight peptides (referred to as light chain,Light chain, L chain, the relative molecular mass of about 25,000) and two identical large molecular weight peptides (called heavy chain, heavy chain, H Chain, relative molecular mass of about 55,000) composed. A natural two heavy chains of IgG molecules are always the same. The goat IgG antibodies can specifically recognize the heavy Chain.
Clonality Polyclonal
Clone Number
Isotype IgG
Purity Caprylic Acid Ammonium Sulfate Precipitation purified
Conjugate Non-conjugated
Stroage Buffer Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form Liquid
Stroage Shipped at 4C. Upon delivery aliquot and store at -20C or -80C. Avoid repeated freeze.
Western blot

All lanes : goat igg heavy chain antibody at 2 µg/ml+goat serum

Lane 1 : goat serum at 1 : 100

Lane 2 : goat serum at 1 : 1000


Rabbit polyclonal to Guinea pig IgG at 1/15000 dilution


Predicted band size : 55 kDa

Observed band size: 50kDa


Why is the actual band size different from the predicted?

Western blotting is a technique that separates proteins based on size - in general, the smaller the protein the faster it migrates through the gel. However, migration is also affected by other factors and so the actual band size observed may differ from that predicted. Common factors include...

         post-translational modification - e.g. phosphorylation, glycosylation etc which increases the size of the protein

         post-translation cleavage - e.g. many proteins are synthesized as pro-proteins, and then cleaved to give the active form, e.g. pro-caspases

         splice variants - alternative splicing may create different sized proteins from the same gene

         relative charge - the composition of amino acids (charged vs non-charged)

multimers - e.g. dimerisation of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands.


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