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993 results found for “charged multivesicular body protein”
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Name :
ThrombinDescription:
Human Thrombin
Product # :
PRO-339Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thrombin was purified from human plasma.
Source
Human Plasma.
Formulation
Lyophilized protein containing mannitol, sodium chloride, calcium chloride.
Biological Activity
The specific activity was found to be 116 US Units/mg protein.
More Info
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Introduction
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
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Physical Appearance
lyophilized powder.
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Stability
Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized human thrombin in sterile a 0.9% NaCl solution at 500U/ml.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SARS Core (340-390)Description:
SARS-Associated Coronavirus Nucleocapsid Core Recombinant, (340-390 a.a)
Product # :
SARS-254Price :
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Shipped with Ice Packs
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Description
The E.Coli derived 32kDa recombinant protein contains the Nucleocapsid core protein 340-390 amino acids immunodominant regions.
Source
Escherichia Coli.
Formulation
50mM Tris-HCl, 60mM NaCl, pH 8 and 50% glycerol.
Purity
SARS Core protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Protein is shipped at ambient temperature. Upon arrival, Store at -20°C.
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Applications
SARS Core antigen is suitable for ELISA and Western blots, excellent antigen for detection of SARS with minimal specificity problems.
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Specificity
SARS Core protein is Immunoreactive with sera of SARS-infected individuals.
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Purification Method
SARS Core protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SDF 1a HumanDescription:
Stromal Cell-Derived Factor-1 Alpha Human Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
Product # :
CHM-262Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 8004 Dalton. The SDF-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentation of 20-80 ng/ml corresponding to a Specific Activity of 12,500-50,000IU/mg.More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Stromal Cell-Derived Factor-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2I HumanDescription:
Ubiquitin-Conjugating Enzyme E2I Human Recombinant
SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.
Product # :
ENZ-341Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBE2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-158 aa) & having a molecular mass of 18.0 kDa. UBE2I is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2I (1mg/ml) contains 50mM HEPES (pH7.4) 150mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Human Ubc9 is homologous to ubiquitin-conjugating enzymes (E2s). However, instead of conjugating ubiquitin, it conjugates a ubiquitin homologue, small ubiquitin-like modifier 1(SUMO-1). And hUbc9 retains striking structural and functional conservation with yeast Ubc9. The ubiquitin-dependent protein degradation system has been recognized as a complete enzymatic pathway that is responsible for the selective degradation of abnormal and short-lived proteins. The conjugation of ubiquitin requires the activities of ubiquitin-activating (E1) and –conjugating (E2) enzymes.
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Synonyms
SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Inhibin a HumanDescription:
Inhibin Alpha Human Recombinant
Product # :
HOR-303Price :
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Shipped with Ice Packs
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Description
Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE analysis.
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.
Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL13 MouseDescription:
BCA-1/BLC Mouse Recombinant (CXCL13)
C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.
Product # :
CHM-030Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.More Info
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Introduction
BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.
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Synonyms
C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.
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Background
What is the molecular weight/Mw of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein has a total Mw of 10kDa.
What is the source or expression system of CXCL13 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL13 MOUSE Protein?
CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL13 MOUSE Protein?
The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.
What is the amino acid sequence of CXCL13 MOUSE Protein?
ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.
What applications can CXCL13 MOUSE Protein be used in?
CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL13 MOUSE Protein?
The endotoxin level is minimal, CXCL13 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Clusterin HumanDescription:
Clusterin Human Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Product # :
CYT-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.
Source
293 cell line (Human embryonic kidney).
Formulation
Filtered (0.4 micron) and lyophilized PBS, pH 7.5.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
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Physical Appearance
Filtered, White, Lyophilized powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
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Amino Acid Sequence
DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 51.27kDa.
What is the source or expression system of CLUSTERIN Protein?
293 cell line
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Collagen-II HumanDescription:
Human Collagen-II
Product # :
PRO-2732Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Collagen-II is a natural protein purified from human cartilage. Collagen- II is purified by proprietary chromatographic techniques.
Source
Human cartilage.
Formulation
Collagen-I was lyophilized without additives.
Purity
> 95.0%.
More Info
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Introduction
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Collagen-II although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-II should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CoV-NL63Description:
Coronavirus NL63 Recombinant
Product # :
SARS-003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Coronavirus NL63 c-terminal nucleoprotein produced in E. coli contains 221-340 amino acids and fused to a 6 a.a. His tag a c-terminal having a total of 130 a.a..
Source
Escherichia Coli.
Formulation
Coronavirus NL63 protein solution is supplied in PBS and 25mM K2CO3.
Purity
Protein is >95% pure as determined by 10% SDS-PAGE (coomassie staining).
More Info
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Introduction
Human coronavirus NL63 also known as HCoV-NL63 is a type of coronavirus that was identified in 2004. Among the associated diseases are mild to moderate upper respiratory tract infections, bronchiolitis, severe lower respiratory tract infection and croup. Coronavirus NL63 appears mainly in young children, the elderly and immunocompromised patients with acute respiratory illness. Coronavirus NL63 has a seasonal association in temperate climates. Coronavirus NL63 is not an emerging virus, but rather one that continually circulates the human population. Transmission of HCoV-NL63 is likely through droplet expulsion from the respiratory tract, which may be cottages when close personal contact occurs. Coronavirus NL63 is able to endure for up to7 days in respiratory secretions and remains infective at room temperature. Once the virus has entered the host it binds to cellular receptors using spike proteins, similar to those found in HIV-1. Coronavirus NL63 is able to use Angiotensin-converting enzyme 2 (ACE2) as an entry receptor to target cells. Since coronavirus NL63 is a positive single-stranded RNA virus, the processes of replication via transcription and translation can be carried out in the cytoplasm of the infected cell.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
GSSQPRADKPSQLKKPRWKRVPTREENVIQCFGPRDFNHNMGDSDLVQNGVDA
KGFPQLAELIPNQAALFFDSEVSTDEVGDNVQITYTYKMLVAKDNKNLPKFIEQISAF
TKPSSIKEMQSLEHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAP2K1 HumanDescription:
Mitogen-Activated Protein Kinase Kinase 1 Human Recombinant
MAP2K1, MEK1, PRKMK1, MKK1, MAPKK 1, MAP kinase kinase 1.
Product # :
PKA-112Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAP2K1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 402 amino acids (1-393a.a.) and having a molecular mass of 44.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MAP2K1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MAP2K1 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The MAP2K1 protein is encoded by the MAP2K1 gene. This enzyme serves as a MAP (mitogen activated protein) kinase, it is a part of the dual specificity protein kinase family. Extracellular signal-regulated kinases such as MAP kinases has an important role in assimilation of various biochemical signals. MAP2K1 is located upstream to the MAP kinases and activates them by multiple intra and extracellular signals. The enzyme serves as a key factor in the signal transduction pathway of MAP kinase, therefore it takes part in the cell development (transcription regulation, proliferation, differentiation etc.).
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Synonyms
MAP2K1, MEK1, PRKMK1, MKK1, MAPKK 1, MAP kinase kinase 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPMPKKKPT PIQLNPAPDG SAVNGTSSAE TNLEALQKKL EELELDEQQR KRLEAFLTQK QKVGELKDDD FEKISELGAG NGGVVFKVSH KPSGLVMARK LIHLEIKPAI RNQIIRELQV LHECNSPYIV GFYGAFYSDG EISICMEHMD GGSLDQVLKK AGRIPEQILG KVSIAVIKGL TYLREKHKIM HRDVKPSNIL VNSRGEIKLC DFGVSGQLID SMANSFVGTR SYMSPERLQG THYSVQSDIW SMGLSLVEMA VGRYPIPPPD AKELELMFGC QVEGDAAETP PRPRTPGRPL SSYGMDSRPP MAIFELLDYI VNEPPPKLPS GVFSLEFQDF VNKCLIKNPA ERADLKQLMV HAFIKRSDAE EVDFAGWLCS TIGLNQPSTP THAAGVHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CALM BovineDescription:
Calmodulin Bovine
Calmodulin, CaM, CALM.
Product # :
PRO-2800Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- source
- formulation
- purity
- More Info
Source
Bovine brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
-
Synonyms
Calmodulin, CaM, CALM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Biochemical and immunochemical investigations.
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Background
Role in Muscle Contraction and Relaxation:
In muscle cells, calmodulin plays a pivotal role in the regulation of contraction and relaxation. It interacts with myosin light-chain kinase during muscle contraction, initiating the process of cross-bridge cycling. Conversely, during muscle relaxation, calmodulin activates the enzyme myosin light-chain phosphatase, leading to the dephosphorylation of myosin and muscle relaxation. This delicate balance is crucial for proper muscle function.
Neuronal Signalling and Synaptic Plasticity:
In neurons, calmodulin is essential for neurotransmitter release and synaptic plasticity. It modulates the activity of proteins involved in vesicle fusion and neurotransmitter release. Additionally, calmodulin-dependent protein kinases (CaMKs) are critical for synaptic plasticity, learning, and memory. The intricate interplay between calmodulin and neuronal proteins underpins the fundamental processes of learning and cognition.
Implications in Disease and Therapeutics:
Dysregulation of calmodulin has been implicated in various diseases, including cardiac arrhythmias and neurodegenerative disorders. Mutations in calmodulin genes can lead to aberrant calcium signalling and cellular dysfunction. Consequently, understanding these molecular mechanisms offers potential therapeutic targets. Researchers are exploring calmodulin inhibitors and modulators for conditions like cardiac arrhythmias, aiming to restore normal cellular function.
Conclusion:
Calmodulin, with its remarkable structural versatility and central role in cellular signalling, epitomizes the complexity of biological regulation. Its influence spans from the fundamental processes of muscle contraction to the intricacies of neuronal signalling. Unravelling the mysteries of calmodulin not only deepens our understanding of basic biological phenomena but also holds the promise of innovative therapeutic interventions. This research illuminates calmodulin's significance, emphasizing its position as a master regulator in the orchestra of cellular life.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BGN MouseDescription:
Biglycan Mouse Recombinant
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
Product # :
PRO-2537Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- More Info
Description
BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 574 amino acids (38-369 a.a.) and having a molecular mass of 64.6kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BGN is expressed with a 242 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.
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Synonyms
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPDEEASGS DTTSGVPDLD SVTPTFSAMC PFGCHCHLRV VQCSDLGLKT VPKEISPDTT LLDLQNNDIS ELRKDDFKGL QHLYALVLVN NKISKIHEKA FSPLRKLQKL YISKNHLVEI PPNLPSSLVE LRIHDNRIRK VPKGVFSGLR NMNCIEMGGN PLENSGFEPG AFDGLKLNYL
RISEAKLTGI PKDLPETLNE LHLDHNKIQA IELEDLLRYS KLYRLGLGHN QIRMIENGSL SFLPTLRELH LDNNKLSRVP AGLPDLKLLQ VVYLHSNNIT KVGINDFCPM GFGVKRAYYN GISLFNNPVP YWEVQPATFR CVTDRLAIQF GNYKKLEPKS CDKTHTCPPC PAPELLGGPS
VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Protein-LDescription:
Protein L Recombinant
SPL.
Product # :
PRO-1790Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Protein-L Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 365 amino acids and having a molecular mass of 40.5 kDa but it migrates with an apparent molecular mass of 45 kDa in SDS-PAGE.The Protein-L is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
The recombinant Protein L is genetically engineered protein and holds 5 IgG-binding regions of protein L and it has the exclusive capability to bind through kappa light chain interactions without interfering with the antibody’s antigen-binding site. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies and it binds to human, mouse, rat and pig IgG.
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Synonyms
SPL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-L in sterile water or saline not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPEEKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IGFBP7 Human, HisDescription:
Insulin Like Growth Factor Binding Protein-7Human Recombinant, His Tag
Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.
Product # :
CYT-809Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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- More Info
- SDS-PAGE
Description
IGFBP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (27-282 a.a.) and having a molecular mass of 28.8kDa.IGFBP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IGFBP7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.
Purity
Greater than 85% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
Insulin-like Growth Factor-Binding Protein 7 (IGFBP7) is a member of the IGFBP family. IGFBP family members are all cysteine rich proteins with conserved cysteine and have an IGFBP domain, a Kazal-like domain and an Ig-like C2-type domain. IGFBP7 is expressed in a broad range of normal human tissues and it mostly shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin. IGFBP7 has a role in skeletal myogenesis by binding to IGF in a manner which inhibits IGF induced differentiation of skeletal myoblasts, without disturbing IGF induced proliferation. Moreover, IGFBP7 suppresses growth and colony formation of prostate and breast cancer cell lines via an IGF independent mechanism, which triggers a delay in the G1 phase of the cell cycle, and increased apoptosis.
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Synonyms
Insulin-like growth factor-binding protein 7, IBP-7, IGF-binding protein 7, IGFBP-7, IGFBP-rP1, MAC25 protein, PGI2-stimulating factor, Prostacyclin-stimulating factor, Tumor-derived adhesion factor, TAF, IGFBP7, MAC25, PSF, AGM, FSTL2, RAMSVPS, IGFBP-7v, IGFBPRP1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSSDTCG PCEPASCPPL PPLGCLLGET RDACGCCPMC ARGEGEPCGG GGAGRGYCAP GMECVKSRKR RKGKAGAAAG GPGVSGVCVC KSRYPVCGSD GTTYPSGCQL RAASQRAESR GEKAITQVSK GTCEQGPSIV TPPKDIWNVT GAQVYLSCEV IGIPTPVLIW NKVKRGHYGV QRTELLPGDR DNLAIQTRGG PEKHEVTGWV LVSPLSKEDA GEYECHASNS QGQASASAKI TVVDALHEIP VKKGEGAEL.
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Background
What is the molecular weight/Mw of IGFBP7 HUMAN, HIS Protein?
IGFBP7 HUMAN, HIS Protein has a total Mw of 28.8kDa.
What is the source or expression system of IGFBP7 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of IGFBP7 HUMAN, HIS Protein?
IGFBP7 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of IGFBP7 HUMAN, HIS Protein?
The biological functionality of IGFBP7 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of IGFBP7 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSSSSDTCG PCEPASCPPL PPLGCLLGET RDACGCCPMC ARGEGEPCGG GGAGRGYCAP GMECVKSRKR RKGKAGAAAG GPGVSGVCVC KSRYPVCGSD GTTYPSGCQL RAASQRAESR GEKAITQVSK GTCEQGPSIV TPPKDIWNVT GAQVYLSCEV IGIPTPVLIW NKVKRGHYGV QRTELLPGDR DNLAIQTRGG PEKHEVTGWV LVSPLSKEDA GEYECHASNS QGQASASAKI TVVDALHEIP VKKGEGAEL.
What applications can IGFBP7 HUMAN, HIS Protein be used in?
IGFBP7 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGFBP7 HUMAN, HIS Protein?
The endotoxin level is minimal, IGFBP7 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Der P1Description:
Der P1 Protein Recombinant
Peptidase 1, Major mite fecal allergen Der p 1, Allergen Der p I, Der p 1, DERP1, Der-P1.
Product # :
ALR-003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- formulation
- purity
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Description
The E.Coli derived recombinant protein contains the Dermatophagoides pteronyssinus Dust Mite Der P1 protein (a.a. 20-320) and fused to a 6 His Tag at C-terminus, having a total Mw of 34.5kDa, pI 5.6.
Source
Escherichia Coli.
Formulation
60mM NaCl and 50mM Tris-HCl pH 8.0.
Purity
Protein is >95% pure as determined by 10% SDS-PAGE (coomassie staining).
More Info
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Introduction
DERP1 is a thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues. DERP1 is a C1 peptidase family member. DERP1 has extensive endopeptidase specificity. DERP1 is N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites. DERP1 causes an allergic reaction in humans. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis. DERP1 binds to IgE in 80% of patients with house dust allergy.
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Synonyms
Peptidase 1, Major mite fecal allergen Der p 1, Allergen Der p I, Der p 1, DERP1, Der-P1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Der-P1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MSIKTFEEYKKAFNKSYATFEDEEAARKNFLESVKYVQSNGGAINHLSDLSLDEFKNRFLMSAEAFEHLKTQFDLNAETNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSAWAFSGVAATESAYLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQRFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLMMIEEYPYVVILHHHHHH.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PYCR1 HumanDescription:
Pyrroline-5-Carboxylate Reductase 1 Human Recombinant
P5C, PRO3, P5CR 1, Pyrroline-5-Carboxylate Reductase 1 mitochondrial, ARCL2B, PYCR, PIG45, PP222, Proliferation-Inducing Protein 45.
Product # :
ENZ-035Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
Description
PYCR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-319a.a.) and having a molecular mass of 35.5kDa.PYCR1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PYCR1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PYCR1 is a universal housekeeping enzyme which catalyzes the NAD(P)H-dependent conversion of pyrroline-5-carboxylate to proline. PYCR1 enzyme also takes a physiologic part in the generation of NADP(+) in certain cell types. PYCR1 forms a homopolymer and localizes to the mitochondrion. Mutations in PYCR1 are the source of cutis laxa autosomal recessive type 2B (ARCL2B).
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Synonyms
P5C, PRO3, P5CR 1, Pyrroline-5-Carboxylate Reductase 1 mitochondrial, ARCL2B, PYCR, PIG45, PP222, Proliferation-Inducing Protein 45.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVGFIGAGQ LAFALAKGFT AAGVLAAHKI MASSPDMDLA TVSALRKMGV KLTPHNKETV QHSDVLFLAV KPHIIPFILD EIGADIEDRH IVVSCAAGVT ISSIEKKLSA FRPAPRVIRC MTNTPVVVRE GATVYATGTH AQVEDGRLME QLLSSVGFCT EVEEDLIDAV TGLSGSGPAY AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLHS EQHPGQLKDN VSSPGGATIH ALHVLESGGF RSLLINAVEA SCIRTRELQS MADQEQVSPA AIKKTILDKV KLDSPAGTAL SPSGHTKLLP RSLAPAGKD
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BMP4 Human, ActiveDescription:
Bone Morphogenetic protein-4 Active Active, Human Recombinant
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-1293Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- biological activity
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Description
Bone Morphogenetic protein-4 Active Human Recombinant produced in E.coli is a homodimer , non-glycosylated, polypeptide chain containing 2x116 amino acids (ser293-arg408) and having a total molecular mass of 26.2kDa. BMP4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a sterile (0.2µm) filtered solution containing 4mM HCL.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 157.2ng/ml corresponding to a specific activity which is 6361 units/mg.
More Info
-
Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BMP4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BMP4 in sterile 4mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions
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Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
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Background
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily.
The superfamily includes large families of growth and differentiation factors.
Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 26.2kDa.
What is the source or expression system of BMP4 Protein?
Escherichia Coli.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The ED50, as calculated by Alkaline phosphatase activity induced in ATDC-5 cells is 157.2ng/ml corresponding to a specific activity which is 6361 units/mg.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAI VQT LVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C1QTNF6 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 6 Human Recombinant
CTRP6, C1QTNF6, ZACRP6, Complement C1q tumor necrosis factor-related protein 6.
Product # :
PRO-655Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
C1QTNF6 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 242 amino acids and having a molecular mass of 27 kDa. The protein contains an extra His tag at N-terminus. The C1QTNF6 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXI9 amino acids 29–259.The C1QTNF6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.23mg/ml in 30mM Acetate Buffer pH-4.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
-
Introduction
C1QTNF6 is a collagen type-IV specific for basement membranes. C1QTNF6 is vital for embryonic development.
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Synonyms
CTRP6, C1QTNF6, ZACRP6, Complement C1q tumor necrosis factor-related protein 6.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MKHHHHHHAS TFDRAVASGC QRCCDSEDPL DPAHVSSASS SGRPHALPEI RPYINITILK GDKGDPGPMG LPGYMGREGP QGEPGPQGSK GDKGEMGSPG APCQKRFFAF SVGRKTALHS GEDFQTLLFE RVFVNLDGCF DMATGQFAAP LRGIYFFSLN VHSWNYKETY VHIMHNQKEA VILYAQPSER SIMQSQSVML DLAYGDRVWV RLFKRQRENA IYSNDFDTYI TFSGHLIKAEDD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HCV NS4 Mosaic Genotype-1Description:
Hepatitis C Virus NS4 Mosaic Genotype-1 Recombinant
Product # :
HCV-257Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- purity
- More Info
Description
The E.coli derived recombinant protein contains the HCV NS4 immunodominant regions, amino acids 1691-1710, 1712-1733 & 1921-1940, fused with a GST tag at N-terminus.
Formulation
1.5M urea, 25mM Tris-HCl, pH 8.0, 0.2% Triton-X & 50% glycerol.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS4 Mosaic Genotype-1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
ELISA, Western blots and Flow-through.
-
Specificity
Immunoreactive with sera of HCV-infected individuals.
-
Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Adiponectin Mouse, TrimericDescription:
Adiponectin Mouse Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-247Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.
Purity
Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SIRPA HumanDescription:
Signal-Regulatory Protein Alpha Human Recombinant
Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.
Product # :
PRO-2080Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIRPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (27-373 a.a) and having a molecular mass of 40.4kDa. SIRPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIRPA protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.
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Synonyms
Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CRP RatDescription:
C-Reactive Protein Rat Recombinant
Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.
Product # :
PRO-1421Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 217 amino acids (20-230 a.a.) and having a molecular mass of 24.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CRP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CRP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HEDMSKQAFV FPGVSATAYV SLEAESKKPL EAFTVCLYAH ADVSRSFSIF SYATKTSFNE ILLFWTRGQG FSIAVGGPEI LFSASEIPEV PTHICATWES ATGIVELWLD GKPRVRKSLQ KGYIVGTNAS IILGQEQDSY GGGFDANQSL VGDIGDVNMW DFVLSPEQIN AVYVGRVFSP NVLNWRALKY ETHGDVFIKP QLWPLTDCCE SHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SOD HumanDescription:
Superoxide Dismutase Human Recombinant
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
Product # :
PRO-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- formulation
- purity
- biological activity
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Description
Recombinant Human Cu/Zn Superoxide Dismutase produced in E.Coli is a non-glycosylated homodimeric polypeptide chain containing 2 x 153 amino acids and having a total molecular mass of 31.6kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The potency per mg was tested by Pyrogallic Acid method and was found to be more than 3,000 Units/mg.
More Info
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Introduction
Human Cu/Zn Superoxide Dismutase (SOD1) catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. SOD1 binds copper and zinc ions and is 1 of 3 isozymes accountable for destroying free superoxide radicals in the body. The encoded protein neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis.
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Synonyms
Superoxide dismutase [Cu-Zn], EC 1.15.1.1, SOD1, SOD, ALS, ALS1, IPOA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SOD although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SOD should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SOD in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ATKAVCVLKG DGPVQGIINF EQKESNGPVK VWGSIKGLTE GLHGFHVHEF GDNTAGCTSA GPHFNPLSRK HGGPKDEERH VGDLGNVTAD KDGVADVSIE DSVISLSGDH CIIGRTLVVH EKADDLGKGG NEESTKTGNA GSRLACGVIG IAQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCN1 HumanDescription:
Cysteine-Rich Angiogenic Inducer 61 Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-164Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.More Info
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Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
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Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD -
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:
Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.Introduction:
Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.Production and Characterization:
Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.Role in Angiogenesis:
CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.Therapeutic Implications:
The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.Conclusion:
Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.
What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.