Recombinant Human beta I Tubulin protein (ab164310)
Key features and details
- Expression system: Wheat germ
- Tags: GST tag N-Terminus
- Suitable for: ELISA, WB
Description
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Product name
Recombinant Human beta I Tubulin protein -
Expression system
Wheat germ -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVY YNEAYGRKYVPRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNN WAKGHYTEGAELIENVLEVVRHESESCDCLQGFQIVHSLGGGTGSGMGTL LMNKIREEYPDRIMNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENADACF CIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADL RKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTM AACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVK VAVCDIPPRGLSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTS EGMDINEFGEAENNIHDLVSEYQQFQDAKAVLEEDEEVTEEAEMEPEDKG H -
Amino acids
1 to 451 -
Tags
GST tag N-Terminus
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Specifications
Our Abpromise guarantee covers the use of ab164310 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
ELISA
Western blot
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Form
Liquid -
Additional notes
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 8.00
Constituents: 0.31% Glutathione, 0.79% Tris HCl
General Info
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Alternative names
- 2810484G07Rik
- beta 1 tubulin
- Beta tubulin 1, class VI
see all -
Function
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain. -
Involvement in disease
Defects in TUBB1 are a cause of macrothrombocytopenia autosomal dominant TUBB1-related (MAD-TUBB1) [MIM:613112]. It is a congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets. -
Sequence similarities
Belongs to the tubulin family. -
Post-translational
modificationsSome glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules. -
Cellular localization
Cytoplasm > cytoskeleton. - Information by UniProt
Images
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab164310 has not yet been referenced specifically in any publications.