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1000 results found for “centrin”
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Name :
ANXA10 HumanDescription:
Annexin A10 Human Recombinant
Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.
Product # :
PRO-1045Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANXA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-324 a.a.) and having a molecular mass of 39.8kDa.ANXA10 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANXA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Annexin A10 (ANXA10) is a member of the annexin family of calcium-binding proteins that contains a few members which are described by a conserved core domain that binds phospholipids in a Ca2+-dependent manner, and a unique amino-terminal region, which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and might be required in the regulation of cellular growth and signal transduction pathways throughout the cell.
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Synonyms
Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.
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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 MGSHMFCGDY VQGTIFPAPN FNPIMDAQML GGALQGFDCD KDMLINILTQ RCNAQRMMIA EAYQSMYGRD LIGDMREQLS DHFKDVMAGL MYPPPLYDAH ELWHAMKGVG TDENCLIEIL ASRTNGEIFQ MREAYCLQYS NNLQEDIYSE TSGHFRDTLM
NLVQGTREEG YTDPAMAAQD AMVLWEACQQ KTGEHKTMLQ MILCNKSYQQ LRLVFQEFQN ISGQDMVDAI NECYDGYFQE LLVAIVLCVR DKPAYFAYRL YSAIHDFGFH NKTVIRILIA RSEIDLLTIR KRYKERYGKS LFHDIRNFAS GHYKKALLAI CAGDAEDY.
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 :
SNCA A30P HumanDescription:
Alpha Synuclein A30P Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-158Price :
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Shipped with Ice Packs
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Description
A-Synuclein A30P Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA A30P protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
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 :
SNCA Delta-NAC HumanDescription:
Alpha Synuclein Delta-NAC Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-161Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A.
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 :
ElcatoninDescription:
Elcatonin
Product # :
HOR-302Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 93.3% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.More Info
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Introduction
Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Elcatonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Elcatonin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Elcatonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.
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 :
CBX1 HumanDescription:
Chromobox Homolog 1 Human Recombinant
Chromobox homolog 1, CBX, M31, HP1-BETA, HP1Hs-beta, MOD1, Heterochromatin protein 1 homolog beta, Modifier 1 protein, p25beta, Chromobox homolog 1 (Drosophila HP1 beta), Heterochromatin protein p25.
Product # :
PRO-876Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CBX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-185) and having a molecular mass of 23.6kDa (molecular weight on SDS-PAGE will appear higher).The CBX1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CBX1 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and
20% Glycerol.Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CBX1 is an enriched heterochromatin which belongs to the heterochromatin protein family. The centromeres related CBX1 identifies and binds histone H3 tails methylated at 'Lys-9', causing epigenetic repression. Collaboration with lamin B receptor (LBR) can impact the relations between the heterochromatin and the inner nuclear membrane. CBX1 has a vital part in the epigenetic control of chromatin structure and gene expression.
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Synonyms
Chromobox homolog 1, CBX, M31, HP1-BETA, HP1Hs-beta, MOD1, Heterochromatin protein 1 homolog beta, Modifier 1 protein, p25beta, Chromobox homolog 1 (Drosophila HP1 beta), Heterochromatin protein p25.
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Physical Appearance
CBX1 is supplied as a 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 MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN TWEPEENLDC PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP KKKKEESEKP RGFARGLEPE RIIGATDSSG ELMFLMKWKN SDEADLVPAK EANVKCPQVV ISFYEERLTW HSYPSEDDDK KDDKN
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 :
CX3CL1 RatDescription:
Fractalkine Rat Recombinant (CX3CL1)
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-005Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fractalkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa.The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FractalkineRat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fractalkine should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Fractalkine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
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Background
What is the molecular weight/Mw of CX3CL1 RAT Protein?
CX3CL1 RAT Protein has a total Mw of 8.7kDa.
What is the source or expression system of CX3CL1 RAT Protein?
Escherichia Coli.
What is the Purity of CX3CL1 RAT Protein?
CX3CL1 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 RAT Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.
What is the amino acid sequence of CX3CL1 RAT Protein?
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
What applications can CX3CL1 RAT Protein be used in?
CX3CL1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 RAT Protein?
The endotoxin level is minimal, CX3CL1 RAT 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 :
LCN1 HumanDescription:
Lipocalin-1 Human Recombinant
Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.
Product # :
ENZ-825Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LCN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (19-176 a.a) and having a molecular mass of 20.1kDa. LCN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Lipocalin-1 (LCN1) belongs to the lipocalin family of small secretory proteins. Lipocalins are extracellular transport proteins, which bind to various hydrophobic ligands. LCN1 protein is the principal lipid binding protein in tears and is overproduced in response to numerous stimuli including infection and stress. LCN1 is a marker for chromosome aneuploidy as well as an autoantigen in Sjogren's syndrome.
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Synonyms
Lipocalin-1, PMFA, TLC, TP, VEGP, Tear lipocalin, Tear prealbumin, Von Ebner gland protein, VEG protein.
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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 MGSHMHHLLA SDEEIQDVSG TWYLKAMTVD REFPEMNLES VTPMTLTTLE GGNLEAKVTM LISGRCQEVK AVLEKTDEPG KYTADGGKHV AYIIRSHVKD HYIFYCEGEL HGKPVRGVKL VGRDPKNNLE ALEDFEKAAG ARGLSTESIL IPRQSETCSP GSD.
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 :
CDC34 Human, HisDescription:
Cell Division Cycle 34 Human Recombinant, His Tag
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
Product # :
ENZ-355Price :
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Shipped with Ice Packs
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Description
CDC34 Human Recombinant protein fused to a 20 amino acid N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-236 a.a.) and having a molecular mass of 28.9 kDa. CDC34 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDC34 (1mg/ml) protein solution contains 20mM Tris-Hcl pH-8, 10% glycerol, 50mM NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CDC34 is important in the control of cell cycle and DNA replication. Cdc34 in association with different E3 complexes, including SCF, has been shown to target many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. Cdc34 substrates that have been characterized include I?B, B-Myb, Wee1, MyoD, ICERII?, ATF5, p27Xic1, and p27Kip1. Additionally, substrates such as ?-catenin, p21Cip1, E2F, cyclin E, and cyclin D are putative substrates of Cdc34 by virtue of their SCF requirement for proteolysis. Cdc34 has been demonstrated to self-associate through a domain in the C-terminus, and is phosphorylated and ubiquitinylated in vivo. This protein is useful for in vitro ubiquitinylation reactions.
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Synonyms
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
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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 MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA RLKFPIDYPY
SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE
YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES.
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 :
LECT1 (214-333) HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.) Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 143 amino acids (214-333) and having a molecular mass of 16.2kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV.
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 :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/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
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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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 MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
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 :
VCPKMT HumanDescription:
Valosin Containing Protein Lysine Methyltransferase Human Recombinant
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
Product # :
PRO-2145Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
VCPKMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a.) and having a molecular mass of 28.2kDa.VCPKMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VCPKMT protein solution (1mg/ml) containing 20mM Phosphate buffer saline (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
VCPKMT is a member of the methyltransferase superfamily. VCPKMT is a protein-lysine N-methyltransferase which specifically trimethylates 'Lys-315' of VCP/p97; this alteration reduces VCP ATPase activity.
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Synonyms
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADTLES SLEDPLRSFV RVLEKRDGTV LRLQQYSSGG VGCVVWDAAI VLSKYLETPE FSGDGAHALS RRSVLELGSG TGAVGLMAAT LGADVVVTDL EELQDLLKMN INMNKHLVTG SVQAKVLKWG EEIEGFPSPP DFILMADCIY YEESLEPLLK TLKDISGFET CIICCYEQRT MGKNPEIEKK YFELLQLDFD FEKIPLEKHD EEYRSEDIHI IYIRKKKSKF PS
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 :
CCL22 Human, HisDescription:
Macrophage-Derived Chemokine Human Recombinant (CCL22), His Tag
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.
Product # :
CHM-367Price :
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- SDS-PAGE
Description
MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 90 amino acids (25-93 a.a.) and having a molecular mass of 10.3 kDa. The MDC is fused to 21 amino acid His-Tag at N-terminus purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MDC protein contains phosphate-buffered Saline (PBS) pH7.4 and 10% glycerol.
Purity
Greater than 95% as determined by Analysis by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer. -
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ.
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Background
What is the molecular weight/Mw of CCL22 HUMAN, HIS Protein?
CCL22 HUMAN, HIS Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL22 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL22 HUMAN, HIS Protein?
CCL22 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL22 HUMAN, HIS Protein?
The biological functionality of CCL22 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL22 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGPYGANMED SVCCRDYVRY RLPLRVVKHF YWTSDSCPRP GVVLLTFRDK EICADPRVPW VKMILNKLSQ
What applications can CCL22 HUMAN, HIS Protein be used in?
CCL22 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL22 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL22 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Streptolysin-ODescription:
Streptolysin-O Streptococcus Pyogenes Recombinant
Streptolysin O, Thiol-activated cytolysin, slo.
Product # :
PRO-2302Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.The Streptolysin-O is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Streptolysin-O protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.
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Synonyms
Streptolysin O, Thiol-activated cytolysin, slo.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Streptolysin-O although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptolysin-O should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Streptolysin-O in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Fibronectin HumanDescription:
Fibronectin Human
Product # :
PRO-448Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Fibronectin produced purified from Human Plasma having a Molecular Weight of 440kDa.
Source
Human Plasma.
Formulation
The Fibronectin was lyophilized from a non sterile 2mg/ml buffer of 10mM sodium phosphate, pH 7.5 and 0.15M NaCl.
Purity
≥ 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the extracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin also takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C.
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Solubility
We suggest reconstituting the 1mg Fibronectin with a chaotropic agent such as urea at room temperature at a concentration of 0.2mg/ml using sterile water. Let stand 1-2 hours. The recommended concentration is 4M-5M urea.
When using the protein as an attachment factor, wash the urea off after attaching the fibronectin to the growth surface (plate or dish).
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 :
Fibronectin RecombinantDescription:
Fibronectin Human Recombinant
Product # :
PRO-2621Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fibronectin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 574 amino acids and having a molecular mass of 62.6kDa. The Fibronectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, with 5 % Trehalose and 0.02 % Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Was measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. The recommended concentration in this application for this effect is typically 1-5 μg/cm2. Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/ml. Optimal concentrations will need to be determined for individual user applications.
More Info
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Introduction
Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Fibronectin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
INHBC HumanDescription:
Inhibin-Beta C Chain Human Recombinant
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
Product # :
HOR-010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The INHBC solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.
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Synonyms
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C 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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS
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 :
CMV Pp52Description:
Cytomegalo Virus Pp52 (UL44) Recombinant
Product # :
CMV-214Price :
Quantity :
Shipping Method :
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Description
The E.coli derived 51 kDa recombinant protein contains the CMV Pp52 (UL44) immunodominant regions, 202-434 amino acids. Recombinant CMV-Pp52 is fused to a 26 kDa GST tag.
Source
Escherichia Coli.
Formulation
50mM Tris pH 7.2, 1mM EDTA and 50% glycerol.
Purity
CMV Pp52 protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
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Stability
CMV Pp52 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
CMV Pp52 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.
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Specificity
Immunoreactive with sera of CMV-infected individuals.
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Purification Method
CMV Pp52 protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CD57 HumanDescription:
CD57 Human Recombinant
B3GAT1, CD57, GLCATP, GLCUATP, HNK1, LEU7, NK-1, NK1, Beta-1,3-glucuronyltransferase 1, Glucuronosyltransferase P, GlcAT-P, UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase, GlcUAT-P.
Product # :
PRO-2618Price :
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Description
CD57 Human Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 549 amino acids (28-334aa) and having a molecular mass of 62.3kDa.CD57 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CD57 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CD57 also called B3GAT1is part of the glucuronyltransferase gene family. CD57 exhibits strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. CD57 takes part in the glucuronyl transfer reaction during the biosynthesis of the carbohydrate epitope HNK-1.
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Synonyms
B3GAT1, CD57, GLCATP, GLCUATP, HNK1, LEU7, NK-1, NK1, Beta-1,3-glucuronyltransferase 1, Glucuronosyltransferase P, GlcAT-P, UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase, GlcUAT-P.
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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
ADPTLAPLLA VHKDEGSDPR RETPPGADPR EYCTSDRDIV EVVRTEYVYT RPPPWSDTLP
TIHVVTPTYS RPVQKAELTR MANTLLHVPN LHWLVVEDAP RRTPLTARLL RDTGLNYTHL
HVETPRNYKL RGDARDPRIP RGTMQRNLAL RWLRETFPRN SSQPGVVYFA DDDNTYSLEL
FEEMRSTRRV SVWPVAFVGG LRYEAPRVNG AGKVVGWKTV FDPHRPFAID MAGFAVNLRL
ILQRSQAYFK LRGVKGGYQE SSLLRELVTL NDLEPKAANC TKILVWHTRT EKPVLVNEGK
KGFTDPSVEI LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV
DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS
NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN
GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.
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 :
Exendin 4Description:
Exendin-4 Recombinant
Product # :
HOR-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Exendin-4 Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 39 amino acids and having a molecular mass of approximately 4.2kDa. Exendin-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
1. Regulates Glucose levels rapidly
2. Reduces Insulin resistance
3. Reduces Glucagon4. Stimulates beta cell growth production.
More Info
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Introduction
Exedin-4 Recombinant is a like peptide-1 receptor agonist. The native hormone is produced in the gut of Gila monster Heloderma suspectrum (a type of reptile found in the desert) that stimulates production without causing threateningly low blood sugar, which can occur after using some anti-diabetes products. Recently, researchers used extracted saliva from gila monsters to create an unprecedented breakthrough in Diabetes Type 2 treatment. Unlike other products taken for type 2 diabetes, Exedin-4 has not been linked with weight gain and actually resulted in weight loss, according to the researchers. Exedin-4 enhances glucose-dependant secretion, suppresses inappropriately elevated secretion and slows gastric emptying in vivo. It also promotes B-cell proliferation and neogenesis in vitro and in animal models. Exedin-4 stimulates an increase in acinar cAMP, without stimulating the release of amylase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Exendin Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Exendin-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Exendin Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HGEGTFTSDL SKQMEEEAVR LFIEWLKNGG PSSGAPPPS.
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 :
CRTAM HumanDescription:
Cytotoxic and Regulatory T Cell Molecule Human Recombinant
Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.
Product # :
PRO-2247Price :
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Description
CRTAM produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 278 amino acids (18-287 a.a.) and having a molecular mass of 31.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CRTAM is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CRTAM protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.
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Synonyms
Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.
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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
SLTNHTETIT VEEGQTLTLK CVTSLRKNSS LQWLTPSGFT IFLNEYPALK NSKYQLLHHS ANQLSITVPN VTLQDEGVYK CLHYSDSVST KEVKVIVLAT PFKPILEASV IRKQNGEEHV VLMCSTMRSK PPPQITWLLG NSMEVSGGTL HEFETDGKKC NTTSTLIIHT YGKNSTVDCI IRHRGLQGRK LVAPFRFEDL VTDEETASDA LERNSLSSQD PQQPTSTVSV TEDSSTSEID KEEKEQTTQD PDLTTEANPQ YLGLARKKSG LEHHHHHH.
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 :
NECTIN2 HumanDescription:
Nectin Cell Adhesion Molecule 2 Human Recombinant
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
Product # :
PRO-2461Price :
Quantity :
Shipping Method :
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Description
NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
NECTIN2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Nectin Cell Adhesion Molecule 2, also known as NECTIN2, is a Ca(2+)-independent cell-cell adhesion molecule which is one of the plasma membrane components of adherens junctions. NECTIN2 takes a vital part in the establishment of homotypic as well as heterotypic cell to cell contacts. NECTIN2 is essential for resisting herpes simplex virus type 2 infection in transfected cells. NECTIN2 is also a possible target for antibody therapy of breast & ovarian cancers. NECTIN2 might be related with human longevity. Two diseases which have been associated with NECTIN2 are Herpes Simplex and Ovarian Cystic Teratoma.
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Synonyms
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Noggin Human, Sf9Description:
Noggin Human Recombinant, Sf9
SYM1, SYNS1, NOG.
Product # :
CYT-1119Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.
More Info
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Introduction
Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Noggin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.
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 :
OAZ1 HumanDescription:
Ornithine Decarboxylase Antizyme 1 Human Recombinant
Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.
Product # :
PRO-1200Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
OAZ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 251 amino acids (1-228) and having a molecular mass of 27.8 kDa.OAZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OAZ1 solution (0.25mg/1ml) 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
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Introduction
OAZ1 is a member of the ODC antizyme family. OAZ1 is auto-regulated expressed by polyamine-enhanced translational frame shifting. OAZ1 negatively controls polyamine synthesis by increasing the negative feedback loop regulating ornithine decarboxylase (ODC) activity. The OAZ1 protein inhibits ornithine decarboxylase and speeds up its detraction.
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Synonyms
Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.
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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 MGSMVKSSLQ RILNSHCFAR EKEGDKPSAT IHASRTMPLL SLHSRGGSSS ESSRVSLHCC SNPGPGPRWC SDAPHPPLKI PGGRGNSQRD HNLSANLFYS DDRLNVTEEL TSNDKTRILN VQSRLTDAKR INWRTVLSGG SLYIEIPGGA LPEGSKDSFA VLLEFAEEQL RADHVFICFH KNREDRAALL RTFSFLGFEI VRPGHPLVPK RPDACFMAYT FERESSGEEE E
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 :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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 MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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.