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1000 results found for “Resistin”
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Name :
ECSIT HumanDescription:
ECSIT homolog Human Recombinant
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
Product # :
PRO-1241Price :
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Description
ECSIT Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (19-217) and having a molecular mass of 24.6 kDa.ECSIT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ECSIT solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.
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Synonyms
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
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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 MGSGTCGAAL TGTSISQVPL PKDSTGAADP PQPHIVGIQS PDQQAALARH NPARPVFVEG PFSLWLRNKC VYYHILRADL LPPEEREVEE TPEEWNLYYP MQLDLEYVRS GWDNYEFDIN EVEEGPVFAM CMAGAHDQAT MAKWIQGLQE TNPTLAQIPV VFRLAGSTRE LQTSSAGLEE PPLPEDHQEE DDNLQRQQQG QS
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 :
OSM RatDescription:
Oncostatin-M Rat Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-169Price :
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Shipped at Room temp
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Description
OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.Citations
More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
Oncostatin-M, OSM, OncoM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M 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
KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.
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 :
PCSK1N HumanDescription:
Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant
ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.
Product # :
PRO-1819Price :
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Description
PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.
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Synonyms
ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.
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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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.
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 :
Super Leptin qA OvineDescription:
Super Leptin Antagonist Ovine Recombinant
Product # :
CYT-1245Price :
Quantity :
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Shipped at Room temp
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Description
Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Ovine leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Ovine leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
BCAR1 HumanDescription:
Breast Cancer Anti-Estrogen Resistance 1 Human Recombinant
CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.
Product # :
PRO-1858Price :
Quantity :
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Description
BCAR1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 407 amino acids (465-848) and having a molecular mass of 43.9kDa. BCAR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCAR1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Breast Cancer Anti-Estrogen Resistance 1 (BCAR1) is a Src family kinase substrate which takes part in a range of cellular events such as migration, survival, transformation, and invasion. BCAR1 plays a vital role for tyrosine kinase-based signaling related to cell adhesion.
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Synonyms
CAS, CAS1, CASS1, CRKAS, P130Cas, Breast cancer anti-estrogen resistance protein 1, CRK-associated substrate, Cas scaffolding protein family member 1, BCAR1.
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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
MGSSHHHHHH SSGLVPRGSH MGSRLQQGVS ATVAHLLDLA GSAGATGSWR SPSEPQEPLV QDLQAAVAAV QSAVHELLEF ARSAVGNAAH TSDRALHAKL SRQLQKMEDV HQTLVAHGQA LDAGRGGSGA TLEDLDRLVA CSRAVPEDAK QLASFLHGNA SLLFRRTKAT APGPEGGGTL HPNPTDKTSS IQSRPLPSPP KFTSQDSPDG QYENSEGGWM EDYDYVHLQG KEEFEKTQKE LLEKGSITRQ GKSQLELQQL KQFERLEQEV SRPIDHDLAN WTPAQPLAPG RTGGLGPSDR QLLLFYLEQC EANLTTLTNA VDAFFTAVAT NQPPKIFVAH SKFVILSAHK LVFIGDTLSR QAKAADVRSQ VTHYSNLLCD LLRGIVATTK AAALQYPSPS AAQDMVE.
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 :
Actin RabbitDescription:
Actin Rabbit
Product # :
PRO-517Price :
Quantity :
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Shipped at Room temp
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Description
Ultra pure Actin consists in the alpha-skeletal muscle isoform and is purified from rabbit striated muscle.The purification method used (according to Spudich & Watts) results in a highly purified protein having a Molecular mass of 43,000 dalton.
Source
Rabbit Muscle.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris/HCl buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% (w/v) SDS.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Actin is a muscle protein localized in the I band of the myofibrils; acting along with myosin, it is responsible for contraction and relaxation of muscle. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans. Its other functions include cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the Lyophilized Actin between 2-8°C, do not freeze. Upon reconstitution Actin 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 Actin in sterile 18MΩ-cm H2O not less than 1mg/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 :
Leptin Human, HisDescription:
Leptin Human Recombinant, His Tag
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-287Price :
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Shipped at Room temp
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Description
Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.
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Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
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 :
Leptin-A TilapiaDescription:
Leptin-A Tilapia Recombinant
Product # :
CYT-1109Price :
Quantity :
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Shipped at Room temp
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Description
Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
Citations
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia 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 Leptin-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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 :
Myostatin Human, HEKDescription:
Myostatin Human Recombinant, HEK
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-833Price :
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Description
Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.
Source
HEK 293.
Formulation
Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
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
HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.
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 :
Art v 1Description:
Major Pollen Allergen Art v 1 Recombinant
Defensin-like protein 1.
Product # :
ALR-014Price :
Quantity :
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Description
Recombinant Art v 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 11,486 Dalton. Art v 1 is expressed with a 5xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Art v 1 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Art v 1, Artemisia vulgaris (mugwort) is a common weed in the Mediterranean area. The significant allergen of mugwort pollen, is a secreted modular glycoprotein with a N-terminal defensin-like and a C-terminal hydroxyproline-rich domain. The reactivity of IgE antibodies is primarily aimed to epitopes located in the N-terminal domain.
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Synonyms
Defensin-like protein 1.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
NECTIN2 HumanDescription:
Nectin Cell Adhesion Molecule 2 Human Recombinant
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
Product # :
PRO-2461Price :
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Description
NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
NECTIN2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.
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Synonyms
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
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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
QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.
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 :
Leptin tA HumanDescription:
Leptin Antagonist Triple Mutant Human Recombinant
Product # :
CYT-352Price :
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Description
Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
Leptin OvineDescription:
Leptin Ovine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-239Price :
Quantity :
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Description
Leptin Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.Citations
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Ovine as a Reference Standard.
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 :
SOST HumanDescription:
Sclerostin Human Recombinant
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-1601Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SOST Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 24-213) containing 200 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 22.8kDa (calculated).
Source
Escherichia Coli.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.03M Acetate buffer pH-4.0.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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Physical Appearance
Filtered White lyophilized (freeze-dried) 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
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASQGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY.
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 :
CETN3 HumanDescription:
Centrin-3 Human Recombinant
CEN3, CEN-3, CETN-3.
Product # :
PRO-533Price :
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Description
CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.
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Synonyms
CEN3, CEN-3, CETN-3.
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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 MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
AIMTGDI.
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 :
Polcalcin Phl p 7Description:
Pollen Allergen Phl p 7 Recombinant
Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.
Product # :
ALR-015Price :
Quantity :
Shipping Method :
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Description
Recombinant Polcalcin Phl p 7 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 9.0 kDa. Polcalcin Phl p 7 is purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Polcalcin Phl p 7 is supplied in 20mM HEPES buffer pH-8.0, 0.2M NaCl, 1mM CaCl2 and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Phl p 7.0101 is a secondary allergen of timothy grass pollen, which is non-glycosylated protein. Grass pollen-sensitized individuals show IgE antibodies in their blood system. Phl p 7.0101 is a calcium binding protein with similar sequence to pollen antigens that exist in different plants, hence, cross-reactions are possible.
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Synonyms
Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
Leptin tA Mouse, PEG (D23L)Description:
Leptin Triple Antagonist (D23L) Pegylated Mouse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1242Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus. The Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Leptin Antagonist Triple Mutant D23L Mouse Recombinant is capable of stimulating proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated recombinant mouse leptin but in vivo it has profound weight reducing effect (as compared to the non-pegylated recombinant mouse leptin), resulting mainly from reduced food intake.
Citations
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes . Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
Vaspin HumanDescription:
Vaspin Recombinant Human
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Product # :
CYT-1132Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
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Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vaspin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vaspin 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 Vaspin 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
LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.
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 :
Vimentin BovineDescription:
Bovine Vimentin
Vimentin, Vim, FLJ36605.
Product # :
PRO-525Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.
Source
Bovine Lens.
Formulation
The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BovineVimentin 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 Bovine Vimentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.
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 :
Leptin RatDescription:
Leptin Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-227Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological activity of Leptin Rat is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.Citations
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-His.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a calibrated solution of Leptin rat as a Reference Standard.
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 :
RCVRN MouseDescription:
Recoverin Mouse Recombinant
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
Product # :
PRO-2547Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recoverin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202a.a.) and having a molecular mass of 25.8kDa. Recoverin Mouse is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.
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Synonyms
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
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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 MGSMGNSKSG ALSKEILEEL QLNTKFTEEE LSAWYQSFLK ECPSGRITRQ EFESIYSKFF PDSDPKAYAQ HVFRSFDANS DGTLDFKEYV IALHMTTAGK PTQKLEWAFS LYDVDGNGTI SKNEVLEIVM AIFKMIKPED VKLLPDDENT PEKRAEKIWA FFGKKEDDKL TEEEFIEGTL ANKEILRLIQ FEPQKVKERI KEKKQ.
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 :
Fibronectin RecombinantDescription:
Fibronectin Human Recombinant
Product # :
PRO-2621Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Fibronectin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 574 amino acids and having a molecular mass of 62.6kDa. The Fibronectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, with 5 % Trehalose and 0.02 % Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Was measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. The recommended concentration in this application for this effect is typically 1-5 μg/cm2. Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/ml. Optimal concentrations will need to be determined for individual user applications.
Citations
More Info
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Introduction
Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin 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 Fibronectin in sterile 18MΩ-cm H2O 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.
- View Data Sheet
Name :
REN Human, HEKDescription:
Renin Human Recombinant, HEK
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
Product # :
PRO-2044Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Renin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Leu24-Arg406) containing a total of 393 amino acids, having a calculated molecular mass of 43.7kDa and fused to a 10 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
REN was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
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Synonyms
Renin, Angiotensinogenase, EC 3.4.23.15, HNFJ2, Angiotensin-Forming Enzyme, Renin Precursor Renal, EC 3.4.23.
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Physical Appearance
Filtered White lyophilized (freeze-dried) 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
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. REN is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
LPTDTTTFKR IFLKRMPSIR ESLKERGVDM ARLGPEWSQP MKRLTLGNTT SSVILTNYMD TQYYGEIGIG TPPQTFKVVF DTGSSNVWVP SSKCSRLYTA CVYHKLFDAS DSSSYKHNGT ELTLRYSTGT VSGFLSQDII TVGGITVTQM FGEVTEMPAL PFMLAEFDGV VGMGFIEQAI GRVTPIFDNI ISQGVLKEDV FSFYYNRDSE NSQSLGGQIV LGGSDPQHYE GNFHYINLIK TGVWQIQMKG VSVGSSTLLC EDGCLALVDT GASYISGSTS SIEKLMEALG AKKRLFDYVV KCNEGPTLPD ISFHLGGKEY TLTSADYVFQ ESYSSKKLCT LAIHAMDIPP PTGPTWALGA TFIRKFYTEF DRRNNRIGFA LAR HHHHHHH HHH.
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.