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1000 results found for “other natural proteins”
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Name :
RPS16 HumanDescription:
Ribosomal Protein S16 Human Recombinant
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
Product # :
PRO-1555Price :
Quantity :
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Shipped with Ice Packs
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Description
RPS16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146) and having a molecular mass of 18.8kDa.RPS16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPS16 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomes are the organelles which catalyze protein synthesis and comprised of a small 40S subunit and a large 60S subunit. Combined, the small 40S and large 60S subunits are composed of 4 RNA types and about 80 structurally distinct proteins. RPS16, a ribosomal protein, is a component of the 40S subunit and a member of the S9P family of ribosomal proteins. RPS16 is situated in the cytoplasm. Just like other genes encoding ribosomal proteins, there are numerous processed pseudogenes of RPS16 spread through the genome.
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Synonyms
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
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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 MGSMPSKGPL QSVQVFGRKK TATAVAHCKR GNGLIKVNGR PLEMIEPRTL QYKLLEPVLL LGKERFAGVD IRVRVKGGGH VAQIYAIRQS ISKALVAYYQ KYVDEASKKE IKDILIQYDR TLLVADPRRC ESKKFGGPGA RARYQKSYR
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 :
IGFBP1 Human, HEKDescription:
Insulin-Like Growth Factor Binding Protein-1 Human Recombinant, HEK
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
Product # :
CYT-1214Price :
Quantity :
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Description
IGFBP1 Human Recombinant is a single, glycosylated, polypeptide chain (26-259 a.a) containing a total of 234 amino acids, having a molecular mass of 25.2 kDa. IGFBP1 is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IGFBP1 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is ≤3 ug/ml, measured by its ability to inhibit proliferation using MCF-7 human breast cancer cells in the presence of Human IGF-1.
More Info
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Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-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
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
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Background
IGFBP-1 (Insulin-like Growth Factor Binding Protein-1) is a vital protein that regulates the actions of insulin-like growth factors (IGFs) in various physiological processes. This research paper aims to investigate the structure, function, and potential therapeutic applications of IGFBP-1, shedding light on its diverse roles in growth regulation and its therapeutic potential.
IGFBP-1 belongs to the IGFBP family and is primarily synthesized and secreted by the liver. It acts as a carrier protein, binding to IGFs in the bloodstream and modulating their availability and distribution to target tissues. By binding to IGFs, IGFBP-1 regulates IGF signaling pathways, influencing cellular growth, differentiation, and metabolism.
The structure of IGFBP-1 comprises an N-terminal domain responsible for IGF binding, followed by linker regions and a C-terminal domain involved in protein-protein interactions. Post-translational modifications, including phosphorylation and glycosylation, further regulate the activity and stability of IGFBP-1.
IGFBP-1 plays a pivotal role in modulating IGF actions in various tissues and physiological contexts. It is involved in fetal development, skeletal growth, and tissue repair. Additionally, IGFBP-1 has been implicated in metabolic regulation, insulin sensitivity, and the pathogenesis of metabolic disorders such as diabetes and obesity.
Therapeutically, IGFBP-1 holds significant promise. Its ability to modulate IGF activity opens avenues for targeted therapies in conditions associated with dysregulated IGF signaling, including cancer. The dysregulation of the IGF pathway is frequently observed in cancer, making IGFBP-1 an attractive candidate for novel therapeutic approaches. Manipulating IGFBP-1 levels or developing IGFBP-1-derived peptides may offer innovative strategies for inhibiting tumor growth or enhancing the effectiveness of existing cancer therapies.
The availability of IGFBP-1 human recombinant proteins has greatly facilitated research and development endeavors. Recombinant IGFBP-1 proteins provide invaluable tools for investigating the interactions between IGFBP-1, IGFs, and other regulatory molecules. They enable detailed exploration of the molecular mechanisms underlying IGFBP-1 function and offer opportunities to unlock its full therapeutic potential.
What is the molecular weight/Mw of IGFBP1 HUMAN, HEK Protein?
IGFBP1 HUMAN, HEK Protein has a total Mw of 25.2kDa.
What is the source or expression system of IGFBP1 HUMAN, HEK Protein?
HEK293 Cells.
What is the Purity of IGFBP1 HUMAN, HEK Protein?
IGFBP1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IGFBP1 HUMAN, HEK Protein?
The ED50 is ≤3 ug/ml, measured by its ability to inhibit proliferation using MCF-7 human breast cancer cells in the presence of Human IGF-1.
What is the amino acid sequence of IGFBP1 HUMAN, HEK Protein?
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
What applications can IGFBP1 HUMAN, HEK Protein be used in?
IGFBP1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGFBP1 HUMAN, HEK Protein?
The endotoxin level is minimal, IGFBP1 HUMAN, HEK 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 :
PVALB HumanDescription:
Parvalbumin Human Recombinant
Parvalbumin alpha, PVALB, D22S749, MGC116759.
Product # :
PRO-004Price :
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Shipped with Ice Packs
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Description
PVALB Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-110 a.a.) and having a molecular mass of 14.6kDa. The PVALB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PVALB solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Parvalbumin alpha (PVALB) is a member of a larger group of EF hand proteins. PVALB is a high affinity calcium ion-binding protein which is structurally and functionally similar to calmodulin and troponin C. Parvalbumin is expressed in a specific population of GABAergic interneurones which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.
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Synonyms
Parvalbumin alpha, PVALB, D22S749, MGC116759.
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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 MGSHMSMTDL LNAEDIKKAV GAFSATDSFD HKKFFQMVGLKKKSADDVKK VFHMLDKDKS GFIEEDELGF ILKGFSPDAR DLSAKETKML MAAGDKDGDG KIGVDEFSTL VAES.
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 :
UNC5B RatDescription:
UNC-5 Netrin Receptor B Rat Recombinant
unc-5 netrin receptor B, Unc5h2, unc-5 homolog 2, Protein unc-5 homolog B, netrin receptor UNC5B precursor, netrin receptor UNC5B, protein unc-5 homolog 2, unc5b.
Product # :
PRO-2659Price :
Quantity :
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Shipped with Ice Packs
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Description
UNC5B Rat Recombinant produced in HEK293 is a single, non-glycosylated polypeptide chain containing 590 amino acids (27-373 a.a) and having a molecular mass of 66.0kDa. UNC5B is fused to a 243 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293.
Formulation
UNC5B protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
UNC-5 Netrin Receptor B or UNC5B, is part of the UNC5 family that has 4 linked receptors and act as a axon guidance molecule Netrin-1 receptor. UNC5B promotes inhibitionleukocyte migration, capillary branching and osteoclast differentiation that are Netrin-1-mediated. UNC5B is responsible for the activation of DAPK1 that can cause apoptosis. The protein takes part in tumorgenesis, development of atherosclerosis and tubular epithelial cells survival when an acute injury in the kidney occurs.
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Synonyms
unc-5 netrin receptor B, Unc5h2, unc-5 homolog 2, Protein unc-5 homolog B, netrin receptor UNC5B precursor, netrin receptor UNC5B, protein unc-5 homolog 2, unc5b.
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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
DGSMGIDSGG QALPDSFPSA PAEQLPHFLL EPEDAYIVKN KPVELHCRAF PATQIYFKCN GEWVSQKGHV TQESLDEATG LRIREVQIEV SRQQVEELFG LEDYWCQCVA WSSSGTTKSR RAYIRIAYLR KNFDQEPLAK EVPLDHEVLL QCRPPEGVPV AEVEWLKNED VIDPAQDTNF LLTIDHNLII RQARLSDTAN YTCVAKNIVA KRRSTTATVI VYVNGGWSSW AEWSPCSNRC GRGWQKRTRT CTNPAPLNGG AFCEGQACQK TACTTVCPVD GAWTEWSKWS ACSTECAHWR SRECMAPPPQ NGGRDCSGTL LDSKNCTDGL CVLNQRTLND PKSRPLEPSG DVEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.
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 :
HSPB7 HumanDescription:
Heat Shock 27kDa Protein Family, Member 7 Human Recombinant
cvHSP, DKFZp779D0968, FLJ32733, HSPB7, CVHSP.
Product # :
HSP-032Price :
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Shipping Method :
Shipped with Ice Packs
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Description
HSPB7 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (1-170 a.a.) and having a molecular mass of 20.7 kDa. HSPB7 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
HSPB7 Human solution containing 20mM Tris HCl pH-8, 0.2M NaCl, 2mM DTT & 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
HSPB7 is part of the Heat shock protein beta family. The HSPB family is one of the more diverse families within the group of HSP families. Several members have chaperone-like activities and/or participate in cytoskeletal stabilization. Several members also show a dynamic, stress-induced translocation to SC35 splicing speckles. HSPB7 constitutively localized to SC35 splicing speckles, determined by its N-terminus. HSPB7 does not support refolding though HSPB1 and HSPB5 chaperone heat unfolded substrates and keet them folding competent.
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Synonyms
cvHSP, DKFZp779D0968, FLJ32733, HSPB7, CVHSP.
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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 MSHRTSSTFR AERSFHSSSS SSSSSTSSSA SRALPAQDPP MEKALSMFSD DFGSFMRPHS EPLAFPARPG GAGNIKTLGD AYEFAVDVRD FSPEDIIVTT SNNHIEVRAE KLAADGTVMN TFAHKCQLPE DVDPTSVTSA LREDGSLTIR ARRHPHTEHV QQTFRTEIKI.
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 :
CXCL10 Human, HisDescription:
IP-10 Human Recombinant (CXCL10), His Tag
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Product # :
CHM-346Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IP-10 His Tag Human Recombinant ?produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (22-98) and having a total molecular mass of 8.5 kDa with an amino-terminal hexahistidine tag. The IP-10 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IP-10 His is supplied in 10mM Tris HCl pH8, 1mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family that is also known as 10 kDa interferon-gamma-induced protein (?-IP10 or IP-10). CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cellsand fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytesand T cells, promotion of T cell adhesion to endothelial cells, anti tumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
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Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein has a total Mw of 8.5kDa.
What is the source or expression system of CXCL10 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL10 HUMAN, HIS Protein?
The biological functionality of CXCL10 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein is composed from 77 amino acids.
What applications can CXCL10 HUMAN, HIS Protein be used in?
CXCL10 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL10 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL10 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.
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Name :
TMEM27 HumanDescription:
Transmembrane Protein 27 Human Recombinant
Collectrin, Transmembrane protein 27, TMEM27, NX17, NX-17.
Product # :
PRO-1581Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TMEM27 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 15-141) containing 137 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 15.64kDa (calculated).
Source
Escherichia Coli.
Formulation
TMEM27 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH-4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Transmembrane Protein 27 (TMEM27) is a type 1 transmembrane protein which is imperative for trafficking amino acid transporters to the apical brush border of proximal tubules. TMEM27 binds to amino acid transporters and regulates their expression on the plasma membrane. The extracellular domain of TMEM27 is cleaved off the surface of beta cells.
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Synonyms
Collectrin, Transmembrane protein 27, TMEM27, NX17, NX-17.
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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 at 37°C. 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. TMEM27 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
MKHHHHHHASELCQPGAENA FKVRLSIRTA LGDKAYAWDT NEEYLFKAMV AFSMRKVPNR EATEISHVLL CNVTQRVSFW FVVTDPSKNH TLPAVEVQSA IRMNKNRINN AFFLNDQTLE FLKIPSTLAP PMDPSVP.
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 :
FHL3 HumanDescription:
Four And A Half LIM Domains 3 Human Recombinant
Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.
Product # :
PRO-1757Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FHL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 33.6kDa. FHL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FHL3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Four and a half LIM domains 3 (FHL3) belongs to a family of proteins containing a four-and-a-half LIM domain, which is a highly conserved double zinc finger motif. FHL3 has been shown to interact with the cancer developmental regulators SMAD2, SMAD3, and SMAD4, the skeletal muscle myogenesis protein MyoD, and the high-affinity IgE beta chain regulator MZF-1. FHL3 is involved in tumor suppression, repression of MyoD expression, and repression of IgE receptor expression. Two transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Four And A Half LIM Domains 3, SLIM2, Skeletal Muscle LIM-Protein 2, FHL-3, SLIM-2, Four And A Half LIM Domains Protein 3, LIM-Only Protein FHL3.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSESFDC AKCNESLYGR KYIQTDSGPY CVPCYDNTFA NTCAECQQLI GHDSRELFYE DRHFHEGCFR CCRCQRSLAD EPFTCQDSEL LCNDCYCSAF SSQCSACGET VMPGSRKLEY GGQTWHEHCF LCSGCEQPLG SRSFVPDKGA HYCVPCYENK FAPRCARCSK TLTQGGVTYR DQPWHRECLV CTGCQTPLAG QQFTSRDEDP YCVACFGELF APKCSSCKRP IVGLGGGKYV SFEDRHWHHN CFSCARCSTS LVGQGFVPDG DQVLCQGCSQ AGP.
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 :
WFDC2 Human, HisDescription:
WAP Four-Disulfide Core Domain 2 Human Recombinant, His Tag
WAP four-disulfide core domain protein 2, Epididymal secretory protein E4, Major epididymis-specific protein E4, Putative protease inhibitor WAP5, WFDC2, HE4, WAP5, EDDM4, dJ461P17.6.
Product # :
PRO-1609Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
WFDC2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (31-124) containing 104 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 11.3kDa (calculated).
Source
Escherichia Coli.
Formulation
WFDC2 filtered (0.4µm) and lyophilized from 0.5mg/ml in PBS buffer, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
WAP four-disulfide core domain protein 2 (WFDC2) is a protease inhibitor, which belongs to the WFDC domain family. WFDC2 is effective with a broad range of proteases, e.g. aspartic, serine or thiol proteases. WFDC2 is expressed in several normal tissues, including the male reproductive system, regions of the respiratory tract and nasopharynx. WFDC2 may be involved in sperm maturation. WFDC2 is also highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines.
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Synonyms
WAP four-disulfide core domain protein 2, Epididymal secretory protein E4, Major epididymis-specific protein E4, Putative protease inhibitor WAP5, WFDC2, HE4, WAP5, EDDM4, dJ461P17.6.
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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 0.5mg/ml and let the lyophilized pellet dissolve completely. WFDC2 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
MKHHHHHHASEKTGVCPELQ ADQNCTQECV SDSECADNLK CCSAGCATFC SLPNDKEGSC PQVNINFPQL GLCRDQCQVD SQCPGQMKCC RNGCGKVSCV TPNF.
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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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- More Info
Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.
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 :
IL 32A Human, HisDescription:
Interleukin-32 alpha Human Recombinant , His Tag
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Product # :
CYT-648Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-131 a.a.) and having a molecular mass of 19.1 kDa. The IL-32 is fused to a 37 amino acid His Tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The IL-32 His Tag protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of interferon gamma.
IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases. -
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
-
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.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMCF PKVLSDDMKK LKARMHQAIE RFYDKMQNAE SGRGQVMSSL AELEDDFKEGYLETVAAYYE EQHPELTPLL EKERDGLRCR GNRSPVPDVE DPATEEPGES FCDKSYGAPR GDKEELTPQK CSEPQSSK.
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 :
ANKRA2 HumanDescription:
Ankyrin Repeat Family A2 Human Recombinant
Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.
Product # :
PRO-2062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313a.a) and having a molecular mass of 36.7kDa. ANKRA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANKRA2 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.
-
Synonyms
Ankyrin Repeat, Family A (RFXANK-Like), 2, ANKRA, RFXANK-Like Protein 2, Ankyrin Repeat Family A Protein 2, ANKRA2.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDTSTNL DIGAQLIVEE CPSTYSLTGM PDIKIEHPLD PNSEEGSAQG VAMGMKFILP NRFDMNVCSR FVKSLNEEDS KNIQDQVNSD LEVASVLFKA ECNIHTSPSP GIQVRHVYTP STTKHFSPIK QSTTLTNKHR GNEVSTTPLL ANSLSVHQLA AQGEMLYLAT RIEQENVINH TDEEGFTPLM WAAAHGQIAV VEFLLQNGAD PQLLGKGRES ALSLACSKGY TDIVKMLLDC GVDVNEYDWN GGTPLLYAVH GNHVKCVKML LESGADPTIE TDSGYNSMDL AVALGYRSVQ QVIESHLLKL LQNIKE.
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 :
NDUFS6 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 6 Human Recombinant
NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.
Product # :
ENZ-725Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.
Source
Escherichia Coli.
Formulation
The NDUFS6 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
NADH Dehydrogenase Fe-S Protein 6 (NDUFS6) is a subunit of the NADH: ubiquinone oxidoreductase (complex I), which is the 1st enzyme complex in the electron transport chain of the mitochondria. This complex operates in the transfer of electrons from NADH to the respiratory chain. NDUFS6 is one of seven subunits in the iron-sulfur protein segment. DNA alterations in NDUFS6 are the cause for mitochondrial complex I deficiency, a disease which results in an extensive assortment of clinical disorders, like adult-onset neurodegenerative disorders and neonatal disease.
-
Synonyms
NADH Dehydrogenase (Ubiquinone) Fe-S Protein 6 13kDa (NADH-Coenzyme Q Reductase), Complex I Mitochondrial Respiratory Chain 13-KD Subunit, NADH Dehydrogenase [Ubiquinone] Iron-Sulfur Protein 6 Mitochondrial, NADH: Ubiquinone Oxidoreductase NDUFS6 Subunit, NADH-Ubiquinone Oxidoreductase 13 KDa-A Subunit, Complex I-13kD-A, CI13KDA.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFGVRVSP TGEKVTHTGQ VYDDKDYRRI RFVGRQKEVN ENFAIDLIAE QPVSEVETRV IACDGGGGAL GHPKVYINLD KETKTGTCGY CGLQFRQHHH
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 :
VAMP1 HumanDescription:
Synaptobrevin-1 Human Recombinant
Vesicle-associated membrane protein 1, SYB1, VAMP-1, Synaptobrevin-1, VAMP1, DKFZp686H12131.
Product # :
PRO-577Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (1-91) and having a molecular mass of 11.9 kDa. The VAMP-1 contains 20 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 1X PBS and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Synaptobrevin 1(Vehicle-associated membrane, VAMP1) is one of the key proteins in the SNARE complex which is involved in regulated exocytosis. Synaptobrevin1 binds to t-SNAREs, syntaxin (STX) and SNAP25, after the fusion of synaptic vesicles to plasma membrane.
-
Synonyms
Vesicle-associated membrane protein 1, SYB1, VAMP-1, Synaptobrevin-1, VAMP1, DKFZp686H12131.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSAPAQPPAE GTEGTAPGGG PPGPPPNMTS NRRLQQTQAQVEEVVDIIRV NVDKVLERDQ KLSELDDRAD ALQAGASQFE SSAAKLKRKY W.
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 :
LZIC HumanDescription:
Leucine Zipper And CTNNBIP1 Domain Containing Human Recombinant
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
Product # :
PRO-1831Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LZIC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (24-111) and having a molecular mass of 12.1 kDa. LZIC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The LZIC solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
LZIC is a member of the CTNNBIP1 family. LZIC protein is universally expressed, with largest levels in kidney and up-regulated in various cases of gastric cancers. LZIC has no interaction with CTNNB1.
-
Synonyms
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASRGKT ETSKLKQNLE EQLDRLMQQL QDLEECREEL DTDEYEETKK ETLEQLSEFN DSLKKIMSGN MTLVDELSGM QLAIQAAISQ AFKTPEVIRL FAKKQPGQLR TRLAEMDRDL MVGKLERDLY TQQKVEILTA LRKLGEKLTA DDEAFLSANA GAILSQFEKV STDLGSGDKI LALASFEVEK TKK.
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 :
CST4 Human, sf9Description:
Cystatin 4 Human Recombinant, sf9
Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.
Product # :
PRO-2250Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 131 amino acids (21-141 a.a.) and having a molecular mass of 15.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions). CST4 is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.
-
Synonyms
Cystatin S, Salivary Acidic Protein 1, Cystatin-SA-III, Cystatin-4, Cystatin 4, Cystatin-S.
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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.
-
Amino Acid Sequence
ADPMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEAHHHHH H.
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 :
S100A1 MouseDescription:
S100 Calcium Binding Protein A1 Mouse Recombinant
Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.
Product # :
PRO-237Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (1-94 a.a) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).S100A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. -
Synonyms
Protein S100-A1, S-100 protein alpha chain, S-100 protein subunit alpha, S100 calcium-binding protein A1, S100a1, S100, S100a, AI266795.
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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 MGSELESAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSGFLDVQK DADAVDKVMK ELDENGDGEV DFKEYVVLVA ALTVACNNFF WETS.
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 :
CEA HumanDescription:
Carcinoembryonic Antigen Human Recombinant
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
- More Info
- SDS-PAGE, Activity Diagram
Description
Recombinant Human Carcinoembryonic Antigen is produced in HEK293 cells (Mammalian expression system) having a molecular mass of 72.4kDa and the target gene encoding Lys35- Ala685 is expressed with a 6xHis tag at the C-terminus.
Source
HEK293 cells.
Formulation
Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Human CEA antibody binds Human CEA protein using a BLI (Bio-Layer Interferometry) assay. Protein A biosensor was used to capture CEA antibody using the Fc portion. Human CEA protein was flowed over the sensor to verify affinity to the antibody which was found to be 1.27nM.SDS-PAGE, Activity Diagram
More Info
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Introduction
Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed. -
Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CEA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CEA 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.
-
Amino Acid Sequence
KLTIESTPFN VAEGKEVLLL VHNLPQHLFG YSWYKGERVD GNRQIIGYVI GTQQATPGPA YSGREIIYPN ASLLIQNIIQ NDTGFYTLHV IKSDLVNEEA TGQFRVYPEL PKPSISSNNS KPVEDKDAVA FTCEPETQDA TYLWWVNNQS LPVSPRLQLS NGNRTLTLFN VTRNDTASYK CETQNPVSAR RSDSVILNVL YGPDAPTISP LNTSYRSGEN LNLSCHAASN PPAQYSWFVN GTFQQSTQEL FIPNITVNNS GSYTCQAHNS DTGLNRTTVT TITVYAEPPK PFITSNNSNP VEDEDAVALT CEPEIQNTTY LWWVNNQSLP VSPRLQLSND NRTLTLLSVT RNDVGPYECG IQNELSVDHS DPVILNVLYG PDDPTISPSY TYYRPGVNLS LSCHAASNPP AQYSWLIDGN IQQHTQELFI SNITEKNSGL YTCQANNSAS GHSRTTVKTI TVSAELPKPS ISSNNSKPVE DKDAVAFTCE PEAQNTTYLW WVNGQSLPVS PRLQLSNGNR TLTLFNVTRN DARAYVCGIQ NSVSANRSDP VTLDVLYGPD TPIISPPDSS YLSGANLNLS CHSASNPSPQ YSWRINGIPQ QHTQVLFIAK ITPNNNGTYA CFVSNLATGR NNSIVKSITV SASGTSPGLS AVDHHHHHH
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 :
S100A3 HumanDescription:
S100 Calcium Binding Protein A3 Human Recombinant
S100-A3, S-100E, S100 calcium-binding protein A3, S100E, S-100A3, Protein S100-A3, Protein S-100E, S100A3.
Product # :
PRO-755Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
S100A3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.9kDa.The S100A3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A3 protein at 1mg/ml in 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.
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Synonyms
S100-A3, S-100E, S100 calcium-binding protein A3, S100E, S-100A3, Protein S100-A3, Protein S-100E, S100A3.
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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).Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MARPLEQAVA AIVCTFQEYA GRCGDKYKLC QAELKELLQK ELATWTPTEF RECDYNKFMS VLDTNKDCEV DFVEYVRSLA CLCLYCHEYF KDCPSEPPCS Q.
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 :
FAM49B HumanDescription:
Family with Sequence Similarity 49, Member B Human Recombinant
BM-009, L1, Protein FAM49B, FAM49B.
Product # :
PRO-1411Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- More Info
Description
FAM49B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347amino acids (1-324 a.a) and having a molecular mass of 39.1kDa. FAM49B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
FAM49B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Family with Sequence Similarity 49, Member B (FAM49B) is a member of the FAM49 family. In the latest genome-wide transcriptional analysis, a gene signature was identified for multiple sclerosis (MS), which reverted back to normal during pregnancy. The reversion was mostly evident for seven genes: SOCS2, TNFAIP3, NR4A2, CXCR4, POLR2J, FAM49B, and STAG3L1, most of which are negative regulators of inflammation.
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Synonyms
BM-009, L1, Protein FAM49B, FAM49B.
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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
MGSSHHHHHH SSGLVPRGSH MGSMGNLLKV LTCTDLEQGP NFFLDFENAQ PTESEKEIYN QVNVVLKDAE GILEDLQSYR GAGHEIREAI QHPADEKLQE KAWGAVVPLV GKLKKFYEFS QRLEAALRGL LGALTSTPYS PTQHLEREQA LAKQFAEILH FTLRFDELKM TNPAIQNDFS YYRRTLSRMR INNVPAEGEN EVNNELANRM SLFYAEATPM LKTLSDATTK FVSENKNLPI ENTTDCLSTM ASVCRVMLET PEYRSRFTNE ETVSFCLRVM VGVIILYDHV HPVGAFAKTS KIDMKGCIKV LKDQPPNSVE GLLNALRYTT KHLNDETTSK QIKSMLQ.
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 :
MLANA HumanDescription:
Melan-A Human Recombinant
MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.
Product # :
PRO-1498Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
MLANA Human Recombinant produced in E. coli is a single polypeptide chain containing 94 amino acids (48-118) and having a molecular mass of 10.4kDa. MLANA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MLANA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Melan-A (MLANA), is engaged in melanosome biogenesis by ensuring the stability of GPR143. MLANA takes part in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is essential to the formation of stage II melanosomes.
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Synonyms
MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.
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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 MGSCRRRNGY RALMDKSLHV GTQCALTRRC PQEGFDHRDS KVSLQEKNCE PVVPNAPPAY EKLSAEQSPP PYSP.
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 :
Streptavidin ProteinDescription:
Streptavidin
Product # :
PRO-283Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
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Description
Streptavidin is a protein produced by Streptomyces avidinii and isolated by purification from fermentation broth. The pure, homogeneous protein shows predominantly one single band in SDS PAGE. Streptavidin consists of 4 identical subunits, each bearing an active binding site for biotin. Streptavidin has a molecular weight of 55kDa.
Source
Bacterium Streptomyces avidinii.
Formulation
The Streptavidin was lyophilized from a 25mg/ml solution in 10 mM potassium phosphate buffer pH 6.5
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Streptavidin although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. For longer storage in dissolved form add 1mM EDTA and/or 0.02 % NaN3 or pass the solution through a sterile filter.Please prevent freeze-thaw cycles.
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Solubility
Gives a clear solution at 10mg/ml in 4.0 mM potassium phosphate pH 6.5
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Specific Activity
The biological activity is 16.8 U/mg, 1 unit binds 1µg biotin.
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 :
DAP HumanDescription:
Death-Associated Protein Human Recombinant
Death-associated protein 1, DAP-1, DAP, DAP1, Death-Associated Protein.
Product # :
PRO-2055Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- formulation
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Description
DAP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102 a.a.) and having a molecular mass of 13.6kDa.DAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DAP protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Death-Associated Protein (DAP) is a proline-rich protein. DAP, which is a negative regulator of autophagy, takes part in the mediation of IFN-gamma-induced cell death.
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Synonyms
Death-associated protein 1, DAP-1, DAP, DAP1, Death-Associated Protein.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSPPEG KLETKAGHPP AVKAGGMRIV QKHPHTGDTK EEKDKDDQEW ESPSPPKPTV FISGVIARGD KDFPPAAAQV AHQKPHASMD KHPSPRTQHI QQPRK.
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 :
GINS4 HumanDescription:
GINS Complex Subunit 4 Protein Human Recombinant
SLD5, GINS complex subunit 4, DNA replication complex GINS protein SLD5.
Product # :
PRO-1270Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
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Description
GINS4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-223 a.a.) and having a molecular mass of 28.2kDa.GINS4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GINS4 protein solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl,20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GINS4, a member of the GINS4/SLD5 family, has a key part in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is significant for GINS complex assembly. GINS complex connects favorably to singlestranded DNA. Recombinant human GINS4 protein, fused to His-tag at N-terminus was purified by using conventional chromatography techniques.
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Synonyms
SLD5, GINS complex subunit 4, DNA replication complex GINS protein SLD5.
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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 MTEEVDFLGQ DSDGGSEEVV LTPAELIERL EQAWMNEKFA PELLESKPEI VECVMEQLEH MEENLRRAKR EDLKVSIHQM EMERIRYVLS SYLRCRLMKI EKFFPHVLEK EKTRPEGEPS SLSPEELAFA REFMANTESY LKNVALKHMP PNLQKVDLFR AVPKPDLDSY VFLRVRERQE NILVEPDTDE QRDYVIDLEK GSQHLIRYKT IAPLVASGAV QLI
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.