Recombinant Phospho-HSP27 (Ser78) Monoclonal Antibody (AN302087L)

Name: Recombinant Phospho-HSP27 (Ser78) Monoclonal Antibody
Brand: Elabscience
SKU: AN302087L
Price: 249.0 USD
Availability: InStock

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Recombinant Phospho-HSP27 (Ser78) Monoclonal Antibody - 1

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	50μL	$ 249.00	- +

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Verified Samples	Verified Samples in WB: HeLa + Anisomycin(-), 2 HeLa+ Anisomycin(+) Verified Samples in IHC: Human breast cancer, Human cervical cancer, Human tonsil Verified Samples in IF: A: HeLa, B HeLa+ Anisomycin(+) Verified Samples in IP: HeLa+Anisomycin (250ng/ml, 30min) cells extracts
Dilution	WB 1:500-1:1000, IHC 1:100-1:500, IF 1:50, IP 1:50-1:100
Isotype	IgG, κ
Host	Rabbit
Reactivity	Human,
Applications	WB, IHC, IF, IP
Clonality	Monoclonal;Recombinant
Immunogen	phosphorylated human HSP27 (Ser78) peptide
Abbre	Phospho-HSP27 (Ser78)
Synonyms	SRP, HSPB, HEL-S, HSP, HSPB1, CMT2F, HEL-S-102, HMN2B, HS.76067, HSP27, HSP28, Hsp25, SRP27, 28 kDa heat shock protein, DKFZp586P1322, epididymis secretory protein Li 102, Estrogen regulated 24 kDa protein, Estrogen-regulated 24 kDa protein, Heat shock 25kDa protein 1, Heat shock 27 kDa protein, Heat shock 27kD protein 1, Heat shock 27kDa protein, Heat shock 27kDa protein 1, Heat shock 28kDa protein 1, Heat Shock Protein 27, Heat shock protein beta 1, Heat shock protein beta-1, heat shock protein family B (small) member 1, Hsp 25, HSP 27, Hsp 28, Hsp B1, Stress responsive protein 27, Stress-responsive protein 27
Swissprot	P04792
Calculated MW	23 kDa
Observed MW	27 kDa The actual band is not consistent with the expectation. Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane.
Cellular Localization	Cytoplasm, Cytoskeleton, Nucleus
Concentration	1 mg/mL
Buffer	PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant.
Purification Method	Protein A purified
Research Areas	Signal Transduction, Cancer, Cardiovascular
Clone No.	A811
Conjugation	Unconjugated
Storage	Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping	Ice bag
background	Hsp27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels. In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-2 as a result of the activation of the p38 MAP kinase pathway. Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers. It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization.