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1000 results found for “epigen”
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Name :
KRT8 Human, HisDescription:
Cytokeratin 8 Human Recombinant, His Tag
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
Product # :
PRO-1567Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KRT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 506 amino acids (1-483 a.a) and having a molecular mass of 56kDa. KRT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT8 protein solution (1mg/ml) containing 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
Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.
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Synonyms
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
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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 MGSMSIRVTQ KSYKVSTSGP RAFSSRSYTS GPGSRISSSS FSRVGSSNFR GGLGGGYGGA SGMGGITAVT VNQSLLSPLV LEVDPNIQAV RTQEKEQIKT LNNKFASFID KVRFLEQQNK MLETKWSLLQ QQKTARSNMD NMFESYINNL RRQLETLGQE KLKLEAELGN MQGLVEDFKN KYEDEINKRT EMENEFVLIK KDVDEAYMNK VELESRLEGL TDEINFLRQL YEEEIRELQS QISDTSVVLS MDNSRSLDMD SIIAEVKAQY EDIANRSRAE AESMYQIKYE ELQSLAGKHG DDLRRTKTEI SEMNRNISRL QAEIEGLKGQ RASLEAAIAD AEQRGELAIK DANAKLSELE AALQRAKQDM ARQLREYQEL MNVKLALDIE IATYRKLLEG EESRLESGMQ NMSIHTKTTS GYAGGLSSAY GGLTSPGLSY SLGSSFGSGA GSSSFSRTSS SRAVVVKKIE TRDGKLVSES SDVLPK.
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 :
TPPP3 HumanDescription:
Tubulin Polymerization-Promoting Protein Family Member 3 Human Recombinant
Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.
Product # :
PRO-1615Price :
Quantity :
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Shipped with Ice Packs
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Description
TPPP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176) and having a molecular mass of 21.4kDa.TPPP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPPP3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TPPP3 is a member of the TPPP family and is found in the cytoplasm. TPPP3 binds tubulin, has microtubule bundling activity takes part in mitosis and cell proliferation.
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Synonyms
Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.
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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 MGSMAASTDM AGLEESFRKF AIHGDPKASG QEMNGKNWAK LCKDCKVADG KSVTGTDVDI VFSKVKGKSA RVINYEEFKK ALEELATKRF KGKSKEEAFD AICQLVAGKE PANVGVTKAK TGGAVDRLTD TSRYTGSHKE RFDESGKGKG IAGRQDILDD SGYVSAYKNA GTYDAKVKK
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 :
GIPC2 HumanDescription:
GIPC PDZ Domain Member 2 Human Recombinant
GIPC PDZ domain containing family member 2, SEMCAP-2, PDZ domain-containing protein GIPC2, semaphorin cytoplasmic domain associated protein 2, semaF cytoplasmic domain associated protein 2, SEMCAP2, FLJ20075.
Product # :
PRO-1035Price :
Quantity :
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Shipped with Ice Packs
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Description
GIPC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-315) and having a molecular mass of 36.9kDa.GIPC2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GIPC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
GIPC2 is a 315 aa protein which is restricted to the cytoplasm and holds one PDZ domain. GIPC2 is expressed in large quantities in colon and kidney and in small quantities in adult liver. GIPC2 has a vital part in human gastric cancer by control of growth factor signaling or cell adhesion.
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Synonyms
GIPC PDZ domain containing family member 2, SEMCAP-2, PDZ domain-containing protein GIPC2, semaphorin cytoplasmic domain associated protein 2, semaF cytoplasmic domain associated protein 2, SEMCAP2, FLJ20075.
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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 MGSHMPLKLR GKKKAKSKET AGLVEGEPTG AGGGSLSASR APARRLVFHA QLAHGSATGR VEGFSSIQEL YAQIAGAFEI SPSEILYCTL NTPKIDMERL LGGQLGLEDF IFAHVKGIEK EVNVYKSEDS LGLTITDNGV GYAFIKRIKD GGVIDSVKTI CVGDHIESIN GENIVGWRHY DVAKKLKELK KEELFTMKLI EPKKAFEIEP RSKAGKSSGE KIGCGRATLR LRSKGPATVE EMPSETKAKA IEKIDDVLEL YMGIRDIDLA TTMFEAGKDK VNPDEFAVAL DETLGDFAFP DEFVFDVWGV IGDAKRRGL
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 :
LGALS10 HumanDescription:
Charcot-Leyden Crystal Protein Human Recombinant
Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.
Product # :
PRO-744Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGALS10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a.) and having a molecular mass of 18.6kDa.LGALS10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Galectin-10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Eosinophil lysophospholipase (CLC) acts on biological membranes to regulate the multifunctional lysophospholipids. CLC is a lysophospholipase expressed in eosinophils and basophils. CLC hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. The CLC protein may possess carbohydrate or IgE-binding activities. CLC is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. CLC may be linked with inflammation and some myeloid leukemias.
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Synonyms
Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.
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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 MSLLPVPYTE AASLSTGSTV TIKGRPLACF LNEPYLQVDF HTEMKEESDI VFHFQVCFGR RVVMNSREYG AWKQQVESKN MPFQDGQEFE LSISVLPDKY QVMVNGQSSY TFDHRIKPEA VKMVQVWRDI SLTKFNVSYL KR.
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 :
CENPQ HumanDescription:
Centromere Protein-Q Human Recombinant
Centromere protein Q, CENPQ, CENP-Q, C6orf139, Centromere Protein-Q.
Product # :
PRO-1815Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CENPQ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-268a.a) and having a molecular mass of 33kDa.CENPQ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CENPQ protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CENPQ is a Component of a CENPH-CENPI-associated centromeric complex which targets CENPA to centromeres and is necessary for proper kinetochore function and mitotic progression. CENPQ takes part in incorporation of newly synthesized CENPA into centromeres using its interaction with the CENPA-NAC complex.
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Synonyms
Centromere protein Q, CENPQ, CENP-Q, C6orf139, Centromere Protein-Q.
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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 MGSMSGKANA SKKNAQQLKR NPKRKKDNEE VVLSENKVRN TVKKNKNHLK DLSSEGQTKH TNLKHGKTAA SKRKTWQPLS KSTRDHLQTM MESVIMTILS NSIKEKEEIQ YHLNFLKKRL LQQCETLKVP PKKMEDLTNV SSLLNMERAR DKANEEGLAL LQEEIDKMVE TTELMTGNIQ SLKNKIQILA SEVEEEEERV KQMHQINSSG VLSLPELSQK TLKAPTLQKE ILALIPNQNA LLKDLDILHN SSQMKSMSTF IEEAYKKLDA S.
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 :
TUBG1 HumanDescription:
Tubulin Gamma 1 Human Recombinant
Tubulin gamma 1, TUBG, TUBGCP1, tubulin gamma polypeptide, Gamma-tubulin complex component 1, GCP-1, gamma-1-tubulin, Tubulin gamma-1 chain.
Product # :
PRO-982Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TUBG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 471 amino acids (1-451 a.a.) and having a molecular mass of 53.3kDa.TUBG1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TUBG1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1M Urea, and 5% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TUBG1 belongs to the tubulin superfamily. TUBG1 localizes to the centrosome and binds to microtubules to create the gamma-tubulin ring complex. TUBG1 facilitates the microtubule nucleation and is essential for microtubule formation and progression of the cell cycle.
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Synonyms
Tubulin gamma 1, TUBG, TUBGCP1, tubulin gamma polypeptide, Gamma-tubulin complex component 1, GCP-1, gamma-1-tubulin, Tubulin gamma-1 chain.
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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 MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE 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.
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Name :
LIF Human, HisDescription:
Leukemia Inhibitory Factor Human Recombinant, His tag
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-1082Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).
Source
Escherichia Coli.
Formulation
LIF filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 20 mM Tris buffer, 20 mM NaCl and 5% w/v trehalose, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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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.
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Amino Acid Sequence
MKHHHHHHAS PLPITPVNAT CAIRHPCHNN LMNQIRSQLA QLNGSANALF ILYYTAQGEP FPNNLDKLCG PNVTDFPPFH ANGTEKAKLV ELYRIVVYLG TSLGNITRDQ KILNPSALSL HSKLNATADI LRGLLSNVLC RLCSKYHVGH VDVTYGPDTS GKDVFQKKKL GCQLLGKYKQ IIAVLAQAF.
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 :
GMNN HumanDescription:
Geminin Human Recombinant
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
Product # :
PRO-579Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% 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
Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.
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Synonyms
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
AKPCI.
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 :
CHGB HumanDescription:
Chromogranin B Human Recombinant
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
Product # :
PRO-824Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
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Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
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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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.
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 :
GPC4 511 aa HumanDescription:
Glypican-4 511 aa Human Recombinant
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
Product # :
PRO-2034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Glypican-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala19-Ser529) containing 521 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 58.7kDa.
Source
Escherichia Coli.
Formulation
Glypican-4 filtered (0.4µm) solution at a concentration of 0.2mg/ml in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.
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Synonyms
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
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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
MKHHHHHHASALLAAELKSK SCSEVRRLYV SKGFNKNDAP LHEINGDHLK ICPQGSTCCS QEMEEKYSLQ SKDDFKSVVS EQCNHLQAVF ASRYKKFDEF FKELLENAEK SLNDMFVKTY GHLYMQNSEL FKDLFVELKR YYVVGNVNLE EMLNDFWARL LERMFRLVNS QYHFTDEYLE CVSKYTEQLK PFGDVPRKLK LQVTRAFVAA RTFAQGLAVA GDVVSKVSVV NPTAQCTHAL LKMIYCSHCR GLVTVKPCYN YCSNIMRGCL ANQGDLDFEW NNFIDAMLMV AERLEGPFNI ESVMDPIDVK ISDAIMNMQD NSVQVSQKVF QGCGPPKPLP AGRISRSISE SAFSARFRPH HPEERPTTAA GTSLDRLVTD VKEKLKQAKK FWSSLPSNVC NDERMAAGNG NEDDCWNGKG KSRYLFAVTG NGLANQGNNP EVQVDTSKPD ILILRQIMAL RVMTSKMKNA YNGNDVDFFD ISDESSGEGS GSGCEYQQCP SEFDYNATDH AGKSANEKAD S.
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 :
CHST10 HumanDescription:
Carbohydrate Sulfotransferase 10 Human Recombinant
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
Product # :
ENZ-894Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.
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Synonyms
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
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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 MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.
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 :
LY6G6F HumanDescription:
Lymphocyte Antigen 6 Complex Locus G6F Human Recombinant
Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.
Product # :
PRO-1782Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LY6G6F Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (17-235) and having a molecular mass of 26.2kDa.LY6G6F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LY6G6F solution 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
The human Lymphocyte Antigen 6 Complex Locus G6F (LY6G6F) protein is a type I transmembrane protein belonging to the immunoglobin (Ig) superfamily, which contains cell-surface proteins involved in the immune system and cellular recognition. The LY6G6F protein has a role in the downstream signal transduction pathways involving GRB2 and GRB7.
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Synonyms
Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.
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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 MGSADNMQAI YVALGEAVEL PCPSPPTLHG DEHLSWFCSP AAGSFTTLVA QVQVGRPAPD PGKPGRESRL RLLGNYSLWL EGSKEEDAGR YWCAVLGQHH NYQNWRVYDV LVLKGSQLSA RAADGSPCNV LLCSVVPSRR MDSVTWQEGK GPVRGRVQSF WGSEAALLLV CPGEGLSEPR SRRPRIIRCL MTHNKGVSFS LAASIDASPA LCAPSTGWDM PW
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 :
Clusterin RatDescription:
Clusterin Rat Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.
Product # :
CYT-437Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Clusterin Rat His-Tagged Fusion Protein, produced in E.coli, is 26.5kDa protein containing 215 amino acid residues of the APO-J Rat and 25 additional amino acid residues: N-terminal fusion of T7-Tag (16AA) and C-terminal fusion of His-Tag (9AA). (Underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.02M Tris buffer and 0.05M NaCl, pH 7.5.
Purity
Greater than 90% as determined by SDS PAGE.
More Info
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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.
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Physical Appearance
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 a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH.
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 26.5kDa.
What is the source or expression system of CLUSTERIN Protein?
Escherichia Coli.
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
MASMTGGQQM GRDPNSSSPF YFWMNGDRID SLLESDRQQS QVLDAMQDSF TRASGIIDTL FQDRFFTHEPQDIHHFSPMG FPHKRPHLLY PKSRLVRSLM PLSHYGPLSF HNMFQPFFDM IHQAQQAMDV QLHSPALQFPDVDFLKEGED DRTVCKEIRH NSTGCLKMKG QCEKCQEILS VDCSTNNPAQ ANLRQELNDS LQVAERLTQQYNELLHSLQS KMLNTSSLLE QALEHHHHHH.
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VAMP8 HumanDescription:
Endobrevin Human Recombinant
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Product # :
PRO-660Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.
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Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.
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 :
PTX3 Human, HEKDescription:
Pentraxin-3 Human Recombinant, HEK
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
Product # :
PRO-2041Price :
Quantity :
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Shipped at Room temp
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Description
Pentraxin-3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Glu18-Ser381) containing a total of 370 amino acids, having a calculated molecular mass of 41kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
PTX3 was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.
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Synonyms
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
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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. PTX3 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
ENSDDYDLMY VNLDNEIDNG LHPTEDPTPC DCGQEHSEWD KLFIMLENSQ MRERMLLQAT DDVLRGELQR LREELGRLAE SLARPCAPGA PAEARLTSAL DELLQATRDA GRRLARMEGA EAQRPEEAGR ALAAVLEELR QTRADLHAVQ GWAARSWLPA GCETAILFPM RSKKIFGSVH PVRPMRLESF SACIWVKATD VLNKTILFSY GTKRNPYEIQ LYLSYQSIVF VVGGEENKLV AEAMVSLGRW THLCGTWNSE EGLTSLWVNG ELAATTVEMA TGHIVPEGGI LQIGQEKNGC CVGGGFDETL AFSGRLTGFN IWDSVLSNEE IRETGGAESC HIRGNIVGWG VTEIQPHGGA QYVSHHHHHH.
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 :
Vaspin Human, HisDescription:
Vaspin Human Recombinant, His Tag
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-459Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vaspin (visceral adipose-specific SERPIN), 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 colorless solution.
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Stability
Liquid Vaspin although stable at 10°C for 1 week, should be stored 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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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.
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 :
COAA E.ColiDescription:
Pantothenate Kinase E.Coli Recombinant
PanK, ts-9, rts.
Product # :
PKA-022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
COAA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-316) and having a molecular mass of 38.9kDa.COAA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The COAA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
COAA is a member of the prokaryotic pantothenate kinase family and it is the first enzyme in the Coenzyme A biosynthetic pathway. COAA phosphorylates pantothenate (vitamin B5) to form 4'-phosphopantothenate. The key factor controlling the intracellular CoA concentration is the regulation of COAA activity by feedback inhibition.
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Synonyms
PanK, ts-9, rts.
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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 MGSHMSIKEQ TLMTPYLQFD RNQWAALRDS VPMTLSEDEI ARLKGINEDL SLEEVAEIYL PLSRLLNFYI SSNLRRQAVL EQFLGTNGQR IPYIISIAGS VAVGKSTTAR VLQALLSRWP EHRRVELITT DGFLHPNQVL KERGLMKKKG FPESYDMHRL VKFVSDLKSG VPNVTAPVYS HLIYDVIPDG DKTVVQPDIL ILEGLNVLQS GMDYPHDPHH VFVSDFVDFS IYVDAPEDLL QTWYINRFLK FREGAFTDPD SYFHNYAKLT KEEAIKTAMT LWKEINWLNL KQNILPTRER ASLILTKSAN HAVEEVRLRK.
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 :
H3F3A HumanDescription:
H3 Histone Family 3A Human Recombinant
RP11-396C23.1, H3.3A, H3F3, Histone H3.3, H3 Histone, Family 3A.
Product # :
PRO-1452Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
H3F3A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (1-136 a.a) and having a molecular mass of 17.7kDa.H3F3A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
H3F3A protein solution (1mg/ml) containing 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
H3F3A is a member of the histone H3 family. Histones are basic nuclear proteins which are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Histones play a significant role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated by a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Two molecules of each of the four core histones H2A, H2B, H3, and H4 form an octamer, around that approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures.
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Synonyms
RP11-396C23.1, H3.3A, H3F3, Histone H3.3, H3 Histone, Family 3A.
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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 MGSMARTKQT ARKSTGGKAP RKQLATKAAR KSAPSTGGVK KPHRYRPGTV ALREIRRYQK STELLIRKLP FQRLVREIAQ DFKTDLRFQS AAIGALQEAS EAYLVGLFED TNLCAIHAKR VTIMPKDIQL ARRIRGERA.
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 :
HAGH HumanDescription:
Hydroxyacylglutathione Hydrolase Human Recombinant
GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.
Product # :
ENZ-034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HAGH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-260a.a.) and having a molecular mass of 31.4kDa.HAGH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HAGH protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.
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Synonyms
GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.
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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 avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKYSI GEPTVPSTLA EEFTYNPFMR VREKTVQQHA GETDPVTTMR AVRREKDQFK MPRD.
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 :
RALA HumanDescription:
V-ral Simian Leukemia Viral Oncogene Homolog A Human Recombinant
Ras-related protein Ral-A, RALA, RAL, MGC48949.
Product # :
PRO-043Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RALA 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 227 amino acids (1-203 a.a.) and having a molecular mass of 25.8kDa. The RALA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RALA solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 100mM NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.
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Synonyms
Ras-related protein Ral-A, RALA, RAL, MGC48949.
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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 MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA EQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC.
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 :
VTN HumanDescription:
Vitronectin Human Recombinant
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
Product # :
PRO-2008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (20-478 a.a) and having a molecular mass of 54.7kDa. VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VTN protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.
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Synonyms
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
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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 MGSDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HL.
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 :
CRIPT HumanDescription:
Cysteine-Rich PDZ-Binding Protein Human Recombinant
Cysteine-rich interactor of PDZ three, cysteine-rich PDZ-binding protein, Cysteine-rich interactor of PDZ3, postsynaptic protein CRIPT, HSPC139.
Product # :
PRO-1105Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRIPT Human Recombinant produced in E. coli is a single polypeptide chain containing 124 amino acids (1-101) and having a molecular mass of 13.7kDa.CRIPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CRIPT solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Cysteine-rich PDZ-binding protein, also known as CRIPT, takes part in the cytoskeletal anchoring of DLG4 in excitatory synapses.
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Synonyms
Cysteine-rich interactor of PDZ three, cysteine-rich PDZ-binding protein, Cysteine-rich interactor of PDZ3, postsynaptic protein CRIPT, HSPC139.
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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
MGSIHHHHHH SSGLVPRGSH MGSMVCEKCE KKLGTVITPD TWKDGARNTT ESGGRKLNEN KALTSKKARF DPYGKNKFST CRICKSSVHQ PGSHYCQGCA YKKGICAMCG KKVLDTKNYK QTSV
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 :
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
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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.
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.
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Name :
RNMT HumanDescription:
RNA (guanine-7-) Methyltransferase Human Recombinant
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
Product # :
ENZ-114Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-476 a.a.) and having a molecular mass of 57kDa.RNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNMT solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 2mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
RNMT is a widely expressed nuclear protein which is a member of the mRNA cap methyltransferase family. Cap-dependent mRNA translation requires the methylation of the mRNA guanosine cap by RNMT. RNMT catalyzes the transfer of a methyl group from AdoMet (S-adenosylmethionine) to the GpppN end of the growing mRNA at the N-7 position, thus producing AdoHyc (S-adenosylhomocysteine) and m7GpppN terminated RNA.
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Synonyms
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
RNMT Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ.
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.