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1000 results found for “calponin”
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Name :
UCHL1 Mouse, ActiveDescription:
Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant, Active
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Product # :
PRO-2424Price :
Quantity :
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Shipped with Ice Packs
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Description
UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 27.2kDa. UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UCHL1 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.
Biological Activity
Specific activity is > 70 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.
More Info
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Introduction
Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.
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Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
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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 MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPAC ALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQF LSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGA SSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.
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 :
Adiponectin ProteinDescription:
Adiponectin Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-280Price :
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- sds-page
Description
The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).
Source
Escherichia Coli.
Formulation
Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.
Purity
Acrp30 purity is greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN. -
Background
Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications
1. Abstract
This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.
2. Introduction
Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.
3. Structure and Signaling of Adiponectin
Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.
4. Biological Functions of Adiponectin
Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.
5. Adiponectin in Disease Pathology
Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.
6. Therapeutic Potential of Adiponectin
Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.
7. Conclusion and Future Perspectives
While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN..
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CTACK MouseDescription:
CTACK Mouse Recombinant (CCL27)
C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.
Product # :
CHM-013Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.More Info
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Introduction
CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.
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Synonyms
C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CTACK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTACK 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 CTACK 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
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.
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Background
What is the molecular weight/Mw of CTACK MOUSE Protein?
CTACK MOUSE Protein has a total Mw of 10.9kDa.
What is the source or expression system of CTACK MOUSE Protein?
Escherichia Coli.
What is the Purity of CTACK MOUSE Protein?
CTACK MOUSE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CTACK MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.
What is the amino acid sequence of CTACK MOUSE Protein?
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.
What applications can CTACK MOUSE Protein be used in?
CTACK MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTACK MOUSE Protein?
The endotoxin level is minimal, CTACK MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL17 RatDescription:
VEGF Co-regulated Chemokine 1 Rat Recombinant
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Product # :
CHM-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.
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 induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.More Info
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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
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Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 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
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
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Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.
What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.
What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 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.
- View Data Sheet
Name :
TAC1 HumanDescription:
Tachykinin-1 Human Recombinant
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.
Product # :
PRO-1338Price :
Quantity :
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Shipped with Ice Packs
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Description
TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.
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Synonyms
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 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 MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.
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 :
CAPZA2 HumanDescription:
Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
Product # :
PRO-1721Price :
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Shipped with Ice Packs
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Description
CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
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Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
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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 MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.
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 :
CCNA2 HumanDescription:
Cyclin-A2 Human Recombinant
Cyclin-A2, Cyclin-A, CCNA2, CCN1, CCNA.
Product # :
PKA-033Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CCNA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-432 a.a) and having a molecular mass of 51.1kDa.CCNA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCNA2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CCNA2 is a member of the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. Various cyclins demonstrate distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. Contrary to cyclin A1, which is present only in germ cells, CCNA2 is expressed in all tissues tested. CCNA2 binds and activates CDC2 or CDK2 kinases, and consequently promotes both cell cycle G1/S and G2/M transitions.
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Synonyms
Cyclin-A2, Cyclin-A, CCNA2, CCN1, CCNA.
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Physical Appearance
Sterile Filtered clear 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 MGSHMLGNSA PGPATREAGS ALLALQQTAL QEDQENINPE KAAPVQQPRT RAALAVLKSG NPRGLAQQQR PKTRRVAPLK DLPVNDEHVT VPPWKANSKQ PAFTIHVDEA EKEAQKKPAE SQKIEREDAL AFNSAISLPG PRKPLVPLDY PMDGSFESPH
TMDMSIVLED EKPVSVNEVP DYHEDIHTYL REMEVKCKPK VGYMKKQPDI TNSMRAILVD WLVEVGEEYK LQNETLHLAV NYIDRFLSSM SVLRGKLQLV GTAAMLLASK FEEIYPPEVA EFVYITDDTY TKKQVLRMEH LVLKVLTFDL AAPTVNQFLT QYFLHQQPAN CKVESLAMFL
GELSLIDADP YLKYLPSVIA GAAFHLALYT VTGQSWPESL IRKTGYTLES LKPCLMDLHQ TYLKAPQHAQ QSIREKYKNS KYHGVSLLNP PETLNL.
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 :
FSCN1 HumanDescription:
Recombinant Human Fascin
Strongylocentrotus Purpuratus, actin-bundling protein, FAN1, HSN, SNL.
Product # :
PRO-527Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FSCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 513 amino acids (1-493 a.a.) and having a molecular mass of 56.7 kDa. The FSCN1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FSCN1 is an actin-bundling protein that is responsible for rigidity to filopodial bundles to efficiently push the membrane forward during cytoskeleton remodeling and cell migration. FSCN1 takes part in the gathering of actin filament bundles present in microspikes, membrane ruffles, and stress fibers. FSCN1 is absent from most normal epithelia though is upregulated in multiple forms of human carcinoma, where its expression associates clinically with a poor prognosis. FSCN1 expression is abundantly found in neurons, glial cells, and endothelial cells.
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Synonyms
Strongylocentrotus Purpuratus, actin-bundling protein, FAN1, HSN, SNL.
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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 MTANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV CLRSHLGRYL
AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA
DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK
DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW
RDRRITLRAS NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND GAYNIKDSTG
KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY.
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 :
GALE HumanDescription:
UDP-Galactose-4-Epimerase Human Recombinant
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
Product # :
ENZ-537Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.
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Synonyms
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
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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 MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.
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 :
Latexin HumanDescription:
Latexin Human Recombinant
LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.
Product # :
ENZ-407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.
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Synonyms
LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.
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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
MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.
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 :
Leptin Receptor ChickenDescription:
Leptin Receptor Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
Product # :
CYT-509Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
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Physical Appearance
Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.
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Stability
Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LGALS2 HumanDescription:
Galectin-2 Human Recombinant
HL14, Gal-2, Beta-galactoside-binding lectin L-14-II, Lactose-binding lectin 2, S-Lac lectin 2.
Product # :
CYT-725Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
LGALS2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids (1-132 a.a.) and having a molecular mass of 16.8 kDa. The LGALS2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-2 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.2M NaCl, 10% glycerol & 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.
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Synonyms
HL14, Gal-2, Beta-galactoside-binding lectin L-14-II, Lactose-binding lectin 2, S-Lac lectin 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 MTGELEVKNM DMKPGSTLKI TGSIADGTDG FVINLGQGTD KLNLHFNPRF SESTIVCNSL DGSNWGQEQR
EDHLCFSPGS EVKFTVTFES DKFKVKLPDG HELTFPNRLG HSHLSYLSVR GGFNMSSFKL KE. -
Background
What is the molecular weight/Mw of LGALS2 HUMAN Protein?
LGALS2 HUMAN Protein has a total Mw of 17kDa.
What is the source or expression system of LGALS2 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS2 HUMAN Protein?
LGALS2 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 HUMAN Protein?
The biological functionality of LGALS2 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMACGLV ASNLNLKPGE CLKVRGEVAS DAKSFVLNLG KDSNNLCLHF NPRFNAHGDA NTIVCNTKED GTWGTEHREP AFPFQPGSIT EVCITFDQAD LTIKLPDGHE FKFPNRLNME AINYMAADGD FKIKCVAFE.
What applications can LGALS2 HUMAN Protein be used in?
LGALS2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 HUMAN Protein?
The endotoxin level is minimal, LGALS2 HUMAN 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 :
LGALS3 Human, HisDescription:
Galectin-3 Human Recombinant, His Tag
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Product # :
CYT-693Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 270 amino acids (1-250 a.a.) and having a molecular mass of 28.3 kDa. The LGALS3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is < 15ug/ml as measured by its ability to agglutinate human red blood cells.sds-page
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
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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 MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.
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Background
What is the molecular weight/Mw of LGALS3 HUMAN, HIS Protein?
LGALS3 HUMAN, HIS Protein has a total Mw of 28.3kDa.
What is the source or expression system of LGALS3 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS3 HUMAN, HIS Protein?
LGALS3 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 HUMAN, HIS Protein?
The ED50 for this effect is < 2.5ug/ml as measured by its ability to agglutinate human red blood cells.
What is the amino acid sequence of LGALS3 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI DLTSASYTMI.
What applications can LGALS3 HUMAN, HIS Protein be used in?
LGALS3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS3 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 :
GrpE E.ColiDescription:
HSP-70 Cofactor (HSP24) E.Coli Recombinant
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
Product # :
HSP-014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
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Synonyms
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
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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
MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.
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 :
HaptoglobinDescription:
Haptoglobin Human Recombinant
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
Product # :
PRO-567Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Haptoglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing fusion protein with His tag and having a total Mw of 33 kDa (4 kDa His-tag).
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin, lung, and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury, and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system (generally the spleen). As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body, haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin, haptoglobin sequesters the iron inside hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis.
Haptoglobin consists of two A- and two B-chains, connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist (Hp 1-1, Hp 2-1, and Hp 2-2). Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active, and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, primary sclerosing cholangitis, susceptibility to idiopathic Parkinson's disease, and a reduced incidence of Plasmodium falciparum malaria. -
Synonyms
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Haptoglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Haptoglobin 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 Haptoglobin 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
L ILGGHLDAKG SFPWQAKMVS HHNLTTGATL INEQWLLTTA KNLFLNHSEN ATAKDIAPTL TLYVGKKQLV EIEKVVLHPN YSQVDIGLIK LKQKVSVNER VMPICLPSKD YAEVGRVGYV SGWGRNANFK FTDHLKYVML PVADQDQCIR HYEGSTVPEK KTPKSPVGVQ PILNEHTFCA GMSKYQEDTC YGDAGSAFAV HDLEEDTWYA TGILSFDKSC AVAEYGVYVK VTSIQDWVQK TIAEN
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 :
Collagen-VI BovineDescription:
Bovine Collagen-VI
Product # :
PRO-2730Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Collagen-VI is a natural protein purified from Bovine placenta. Bovine Collagen-VI is purified by proprietary chromatographic techniques.
Source
Bovine placenta.
Formulation
Collagen-VI was lyophilized without additives.
Purity
> 90.0%.
More Info
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Introduction
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Collagen-VI although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-VI should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SCGB1A1 MouseDescription:
Uteroglobin Mouse Recombinant
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
Product # :
CYT-746Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 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
DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BGN Human, Sf9Description:
Biglycan Human Recombinant, Sf9
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
Product # :
PRO-2536Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic fibroblast adipose-like cells.
More Info
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Introduction
Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.
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Synonyms
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
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Physical Appearance
Sterile filtered colorless solution.
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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
ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.
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 :
ITGB1BP3 HumanDescription:
Integrin Beta 1 Binding Protein 3 Human Recombinant
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 2.
Product # :
PRO-1177Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
ITGB1BP3 Human Recombinant produced in E. coli is a single polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 28.4 kDa.ITGB1BP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ITGB1BP3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Nicotinamide riboside kinase 2 (ITGB1BP3) is a member of the uridine kinase family and NRK subfamily. ITGB1BP3 catalyzes the phosphorylation of nicotinic acid riboside and nicotinamide riboside to create nicotinic acid mononucleotide and nicotinamide mononucleotide. ITGB1BP3 reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. ITGB1BP3 is involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. ITGB1BP3 also has a role in the regulation of terminal myogenesis.
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Synonyms
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 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 MGSMKLIVGI GGMTNGGKTT LTNSLLRALP NCCVIHQDDF FKPQDQIAVG EDGFKQWDVL ESLDMEAMLD TVQAWLSSPQ KFARAHGVSV QPEASDTHIL LLEGFLLYSY KPLVDLYSRR YFLTVPYEEC KWRRSTRNYT VPDPPGLFDG HVWPMYQKYR QEMEANGVEV VYLDGMKSRE ELFREVLEDI QNSLLNRSQE SAPSPARPAR TQGPGRGCGH RTARPAASQQ DSM
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 :
GALNT1 MouseDescription:
Polypeptide N-Acetylgalactosaminyltransferase 1 Mouse Recombinant
Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 1.
Product # :
ENZ-1066Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559 a.a.) and having a molecular mass of 60.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GALNT1 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
Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) , is part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.
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Synonyms
Polypeptide N-acetylgalactosaminyltransferase 1, Polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, Protein-UDP acetylgalactosaminyltransferase 1, polypeptide N-acetylgalactosaminyltransferase 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
ADPGLPAGDV LELVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSRGQVITF LDAHCECTAG WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS SRLGLRRKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH VNSNQCLDKA TEEDSQVPSI RDCTGSRSQQ WLLRNVTLPE IFHHHHHH .
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 :
CES1D MouseDescription:
Carboxylesterase 1D Mouse Recombinant
Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.
Product # :
ENZ-1007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CES1D Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 555 amino acids (19-565 a.a) and having a molecular mass of 60.9kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1D is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CES1D protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 80,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to pnitrophenol per minute at pH 7.5 at 37C.More Info
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Introduction
Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.
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Synonyms
Carboxylesterase 1D, Carboxylesterase 3 (EC:3.1.1.1, EC:3.1.1.67), Fatty acid ethyl ester synthase, FAEE synthase, Triacylglycerol hydrolase, TGH, CES1D.
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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
YPSSPPVVNT VKGKVLGKYV NLEGFTQPVA VFLGVPFAKP PLGSLRFAPP QPAEPWSFVK NTTSYPPMCS QDAVGGQVLS ELFTNRKENI PLQFSEDCLY LNIYTPADLT KNSRLPVMVW IHGGGLVVGG ASTYDGLALS AHENVVVVTI QYRLGIWGFF STGDEHSRGN WGHLDQVAALRWVQDNIANF GGNPGSVTIF GESAGGFSVS VLVLSPLAKN LFHRAISESG VSLTAALITT DVKPIAGLVA TLSGCKTTTS AVMVHCLRQK TEDELLETSL KLNLFKLDLL GNPKESYPFL PTVIDGVVLP KAPEEILAEK SFSTVPYIVG INKQEFGWII PTLMGYPLAE GKLDQKTANSLLWKSYPTLK ISENMIPVVA EKYLGGTDDL TKKKDLFQDL MADVVFGVPS VIVSRSHRDA GASTYMYEFE YRPSFVSAMR PKAVIGDHGD EIFSVFGSPF LKDGASEEET NLSKMVMKFW ANFARNGNPN GGGLPHWPEY DQKEGYLKIG ASTQAAQRLK DKEVSFWAEL RAKESAQRPSHREHVELLEH HHHHH.
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 :
CNDP1 Human, ActiveDescription:
CNDP Dipeptidase 1 Human Recombinant, Active
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
Product # :
ENZ-1022Price :
Quantity :
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Shipped with Ice Packs
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Description
CNDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507 a.a.) and having a molecular mass of 54.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).CNDP1 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >3,000 pmol/min/ug, and as measured by the hydrolysis of carnosine per minute at pH6.8 at 25°C.More Info
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Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
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Synonyms
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
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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
SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.
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 :
GLP 1 HumanDescription:
Human Glucagon Like Peptide-1
GLP1, Glucagon Like Peptide-1, Incretin hormone.
Product # :
HOR-284Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glucagon Like Peptide-1 is a single, non-glycosylated, polypeptide chain containing 30 amino acids and having a molecular mass of 3297.7 Dalton.The GLP-1 is purified by proprietary chromatographic techniques.
Formulation
The GLP-1 peptide was lyophilized with no additives.
Purity
Greater than 96.0% as determined by RP-HPLC.
More Info
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Introduction
Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety. -
Synonyms
GLP1, Glucagon Like Peptide-1, Incretin hormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-1 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 Glucagon Like Peptide-1 in sterile H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-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.
- View Data Sheet
Name :
Ara h 2.0201Description:
Allergen Ara h 2.0201 (Conglutin-7) Recombinant
Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.
Product # :
ALR-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Allergen Ara h 2.0201 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 20,000 Dalton. Ara h 2.0201 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Ara h 2.0201 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.
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Synonyms
Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.