TPM1 Antibody

Code: CSB-PA024104ZA01RB

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Size:

0.1ml

0.1ml1ml

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Species Reactivity: Oryctolagus cuniculus

Raised in: Rabbit

Application: ELISA, WB (ensure identification of antigen)

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Target Background

Product Details

Uniprot NO.

P58772

Target Names

TPM1

Alternative Names

Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1), TPM1, TPMA

Raised in

Rabbit

Species Reactivity

Oryctolagus cuniculus

Immunogen

Recombinant Oryctolagus cuniculus TPM1 protein

Conjugate

Non-conjugate

Isotype

IgG

Purification Method

Antigen Affinity Purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Tested Applications

ELISA, WB (ensure identification of antigen)

Lead Time

Made-to-order (12-14 weeks)
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Value-added Deliverables

① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);

Quality Guarantee

① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;

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Target Background

Function(From Uniprot)

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

Gene References into Functions

The results indicate that cross-linking significantly affects properties of Tpm and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm in human heart diseases. PMID:27856252
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions PMID:27480605
analysis of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1 PMID:27956029
We propose that TR100 acts to compromise the integrity of Tpm cables rather than prevent overlap complex formation. Our data suggests that TR100 is incorporated into the growing actin-Tpm co-polymer given that its effects cannot be observed on pre-formed Tpm3.1/actin filaments PMID:26804624
Maximal Ca(2+) activated force was the same in alphaalphaTm versus betabetaTm myofibrils, but betabetaTm myofibrils showed a marked slowing of relaxation and an impairment of regulation under resting conditions PMID:25380572
Tmod1 and Tmod3 showed somewhat different tropomyosin-binding site utilization. PMID:24922351
Thermal denaturation of rabbit cardiac alpha,alpha-tropomyosin is monitored at neutral pH and compared to shark tropomyosin, showing that amino acid substitutions predicted to be unfavorable in one temperature regime are desirable in another. PMID:21707054
The rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin, was measured. PMID:21575577
a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed. PMID:21320445