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MilliporeSigma

SAB4300527

Sigma-Aldrich

Anti-RPS6KB1 (Ab-424) antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-PS6K antibody produced in rabbit, Anti-S6K antibody produced in rabbit, Anti-S6K1 antibody produced in rabbit, Anti-STK14A antibody produced in rabbit, Anti-ribosomal protein S6 kinase, 70kDa, polypeptide 1 antibody produced in rabbit

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

Key Documents

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biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~70 kDa
 ~85 kDa

species reactivity

human, mouse, rat

concentration

1 mg/mL

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50-1:100
indirect immunofluorescence: 1:100-1:200
western blot: 1:500-1:1000

isotype

IgG

immunogen sequence

(P-V-S-P-V)

NCBI accession no.

NP_003152.1

UniProt accession no.

P23443

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... RPS6KB1(6198)

General description

RPS6KB1 phosphorylates the Ribosomal Protein-S6. Activation of RPS6KB1 requires a complex, ordered series of conformational changes and phosphorylation reactions. While the role of sequential, multi-site phosphorylation has been extensively detailed, characterization of the priming step required to initiate this cascade has remained elusive. Probably this priming process is dependent on calcium. Calcium-dependent regulation of RPS6KB1 does not specifically target Thr-229 and Thr-389, the key regulatory phosphorylation sites; rather, calcium chelation results in a global inhibition of RPS6KB1 phosphorylation. The initial calcium-dependent process is required to release an inhibitory interaction between the C- and N-termini of RPS6KB1, thus allowing phosphorylation of key domains. The priming event involves formation of a calcium-dependent protein complex that releases the interaction between the N- and C-termini. RPS6KB1 is then accessible for activation by the kinases that target the known regulatory phosphorylation sites .

Immunogen

Peptide sequence around aa. 422-426 (P-V-S-P-V), according to the protein RPS6KB1.

Features and Benefits

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Physical form

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
951421276

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Atsushi Yamamoto et al.
Biology of reproduction, 91(1), 7-7 (2014-05-24)
Autophagy is a dynamically regulated intracellular degradation system that is important for cellular processes such as amino acid production during starvation and intracellular quality control. Previously, we reported that autophagy is suppressed in oocytes but is rapidly up-regulated after fertilization.
Ana Salvador-Adriano et al.
American journal of physiology. Endocrinology and metabolism, 306(12), E1442-E1448 (2014-05-08)
We have reported an early decrease in glycemia in rats fed a biotin-deficient diet with reduced cellular ATP levels, suggesting increased insulin sensitivity. Here, we show that biotin-deprived rats are more tolerant of glucose, as shown by both oral and
Lasse Boding et al.
European journal of immunology, 44(10), 3109-3118 (2014-07-22)
Midline 1 (MID1) is a microtubule-associated ubiquitin ligase that regulates protein phosphatase 2A activity. Loss-of-function mutations in MID1 lead to the X-linked Opitz G/BBB syndrome characterized by defective midline development during embryogenesis. Here, we show that MID1 is strongly upregulated
Cyrille de Joussineau et al.
Human molecular genetics, 23(20), 5418-5428 (2014-05-29)
Primary pigmented nodular adrenocortical disease (PPNAD) is associated with inactivating mutations of the PRKAR1A tumor suppressor gene that encodes the regulatory subunit R1α of the cAMP-dependent protein kinase (PKA). In human and mouse adrenocortical cells, these mutations lead to increased

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