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1000 results found for “Calumenin”
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Name :
Leptin Receptor ChickenDescription:
Leptin Receptor Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
Product # :
CYT-509Price :
Quantity :
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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.Citations
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.
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Name :
SEPT2 HumanDescription:
Septin-2 Human Recombinant
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
Product # :
PRO-255Price :
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Description
SEPT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 381 amino acids (1-361 a.a.) and having a molecular mass of 43.6kDa. SEPT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEPT2 solution (0.25mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SEPT2 is a GTPase which is mandatory for cytokinesis and related to exocytosis. Septin-2 protein is able to hetero-oligomerize with Septin6, 7 and in addition takes part in the organization of new growth in organisms. SEPT2 is associated with a Tau-based paired helical filament core and contributes to the creation of neurofibrillary tangle as integral constituents of paired helical filaments.
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Synonyms
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
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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 MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT DLYPERVISG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH V.
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 :
UBQLN2 HumanDescription:
Ubiquilin 2 Human Recombinant
UBQLN2, Ubiquilin 2, CHAP1, PLIC2, Protein Linking IAP With Cytoskeleton 2, Ubiquitin-Like Product Chap1/Dsk2, ALS15, N4BP4, NEDD4 Binding Protein 4, Nedd4 Binding Protein 4, DSK2 Homolog, Ubiquilin-2, HRIHFB2157, HPLIC-2, PLIC-2, DSK2.
Product # :
PRO-2228Price :
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Description
UBQLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 647 amino acids (1-624 a.a) and having a molecular mass of 68.1kDa. UBQLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBQLN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ubiquilin-2, also known as UBQLN2 contains an N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. UBQLN2 is physically linked with proteasomes as well as ubiquitin ligases, and therefore is considered to functionally connect the ubiquitination machinery to the proteasome in order to affect in vivo protein degradation. Furthermore, UBQLN2 binds the ATPase domain of the Hsp70-like Stch protein. Among the diseases which are associated with UBQLN2: Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia as well as Amyotrophic lateral sclerosis type 15.
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Synonyms
UBQLN2, Ubiquilin 2, CHAP1, PLIC2, Protein Linking IAP With Cytoskeleton 2, Ubiquitin-Like Product Chap1/Dsk2, ALS15, N4BP4, NEDD4 Binding Protein 4, Nedd4 Binding Protein 4, DSK2 Homolog, Ubiquilin-2, HRIHFB2157, HPLIC-2, PLIC-2, DSK2.
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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 MGSMAENGES SGPPRPSRGP AAAQGSAAAP AEPKIIKVTV KTPKEKEEFA VPENSSVQQF KEAISKRFKS QTDQLVLIFA GKILKDQDTL IQHGIHDGLT VHLVIKSQNR PQGQSTQPSN AAGTNTTSAS TPRSNSTPIS TNSNPFGLGS LGGLAGLSSL GLSSTNFSEL QSQMQQQLMA SPEMMIQIME NPFVQSMLSN PDLMRQLIMA NPQMQQLIQR NPEISHLLNN PDIMRQTLEI ARNPAMMQEM MRNQDLALSN LESIPGGYNA LRRMYTDIQE PMLNAAQEQF GGNPFASVGS SSSSGEGTQP SRTENRDPLP NPWAPPPATQ SSATTSTTTS TGSGSGNSSS NATGNTVAAA NYVASIFSTP GMQSLLQQIT ENPQLIQNML SAPYMRSMMQ SLSQNPDLAA QMMLNSPLFT ANPQLQEQMR PQLPAFLQQM QNPDTLSAMS NPRAMQALMQ IQQGLQTLAT EAPGLIPSFT PGVGVGVLGT AIGPVGPVTP IGPIGPIVPF TPIGPIGPIG PTGPAAPPGS TGSGGPTGPT VSSAAPSETT SPTSESGPNQ QFIQQMVQAL AGANAPQLPN PEVRFQQQLE QLNAMGFLNR EANLQALIAT GGDINAAIER LLGSQPS.
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 :
BCL7A HumanDescription:
B-cell CLL/lymphoma 7A Human Recombinant
B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.
Product # :
PRO-1318Price :
Quantity :
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Shipped with Ice Packs
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Description
BCL7A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear higher).BCL7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BCL7A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 2mM EDTA.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
B-cell CLL/lymphoma 7A (BCL7A) is a member of the BCL7 family. BCL7A is directly involved, with Myc and IgH, in a three-way gene translocation in a Burkitt lymphoma cell line. Thru gene translocation, the N-terminal region of the BCL7A gene is disrupted, which is assumed to be connected to the pathogenesis of a subset of high-grade B cell non-Hodgkin lymphoma. The N-terminal portion involved in the translocation includes the region which shares a compelling sequence similarity with those of BCL7B and BCL7C. Chromosomal anomalies involving BCL7A may be a cause of B-cell non-Hodgkin lymphoma.
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Synonyms
B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.
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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 MGSMSGRSVR AETRSRAKDD IKRVMAAIEK VRKWEKKWVT VGDTSLRIYK WVPVTEPKVD DKNKNKKKGK DEKCGSEVTT PENSSSPGMM DMHDDNSNQS SIADASPIKQ ENSSNSSPAP EPNSAVPSDG TEAKVDEAQA DGKEHPGAED ASDEQNSQSS MEHSMNSSEK VDRQPSGDSG LAAETSAISQ DLEGVPPSKK MKLEASQQNS EEM.
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 :
p59-Fyn HumanDescription:
p59-Fyn Human Recombinant
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
Product # :
PRO-506Price :
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Description
p59-Fyn Human Recombinant (a.a. 23-216) expressed in E.coli, shows a 50 kDa SDS-PAGE (Including GST tag).The p59-Fyn is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
p59-Fyn in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.
Citations
More Info
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Introduction
p59-Fyn is a member of the protein-tyrosine kinase oncogene family. p59fyn is a membrane-associated non-receptor protein tyrosine kinase that belongs to the Src-family of kinases. p59-Fyn encodes a membrane-associated tyrosine kinase which is implicated in the control of cell growth. p59-Fyn associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. The unique N-terminal domain of p59fyn interacts with the CD3 and eta chains of the TcR. p59fyn can bind other proteins (p82 and p116) through its SH2 and SH3 domains, which may act as substrates or regulators of fyn activity. p59fyn is highly expressed in brain suggesting that it may have a role in the sensory nervous network and in myelination at early stages of CNS formation. Distinct isoforms exist due to alternative splicing.
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Synonyms
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Applications
• ELISA
• Inhibition Assays
• Western Blotting.
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 :
FGF 2 HumanDescription:
Fibroblast Growth Factor-Basic Human Recombinant
Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-218Price :
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Shipped at Room temp
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Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.The FGF-b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.
Purity
Greater than 98.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.
Citations
More Info
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Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The HPR -binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
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Synonyms
Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibroblast Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b 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 Fibroblast Growth Factor Basic 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
AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.
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Background
FGF 2 HUMAN: Insights into Fibroblast Growth Factor-2
Basic Fibroblast Growth Factor or FGF 2 HUMAN is a protein with crucial roles in cell growth, tissue repair, and embryonic development. This is part of the larger fibroblast growth factor family and is vital for various biological processes, including the modulation of cell survival activities.
Production and Properties
Produced in E. coli, FGF 2 is a non-glycosylated polypeptide chain possessing 154 amino acids with a molecular weight of about 17.2 kDa. It is purified through advanced chromatographic techniques, ensuring high purity and activity for laboratory use.
Physical Characteristics and Preparation
The physical form of FGF 2 HUMAN is a sterile, white lyophilized powder. For experimental use, it is reconstituted with sterile water to at least 100µg/ml. This reconstitution is crucial for maintaining the integrity and effectiveness of the protein in various research applications.
Storage and Handling
To maintain stability, lyophilized FGF 2 should be stored at -18°C and used within three weeks if kept at room temperature. Once reconstituted, it should be kept at 4°C and used within 2-7 days or stored at -18°C for longer-term storage.
Proper handling and avoiding repeated freeze-thaw cycles are essential to preserve the protein's functionality.
Purity and Biological Activity
FGF 2 is characterized by a purity greater than 98%, verified by SDS-PAGE analysis. Its biological activity is primarily defined by its efficacy in promoting the proliferation of specific cell lines, with an effective dose (ED50) typically below 0.1 ng/ml.
Research Applications and Impact
In the research context, FGF 2 is used extensively to study its effects on cell migration, proliferation, and angiogenesis. Moreover, its role in disease models, particularly in cancer and tissue repair studies, makes it a valuable resource for developing new therapeutic approaches.
Usage Guidelines
FGF 2 HUMAN is strictly for laboratory research use and is not suitable for drug development, food production, or cosmetic applications. Researchers are advised to comply with safety and handling guidelines to ensure that experiments are conducted under optimal conditions.
The Broad Impact on Development and Disease
FGF-2 is known for its multifunctional role across numerous biological processes such as tissue repair, embryonic development, angiogenesis, and even tumorigenesis.
This growth factor, existing in various synonymous forms such as Basic FGF, FGF-b, and HBGF-2, is essential in cellular processes that underpin both health and disease.
Furthermore, FGF-2's ability to bind to cellular receptors triggers a cascade of signaling pathways, including PI3K/Akt, MAPK/ERK, and PLCγ, which in turn influence cell growth, migration, and survival.
These pathways are pivotal in mediating the factor's diverse effects on cell behavior, contributing to its critical roles in wound healing, angiogenesis, and tissue remodeling.
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.2kDa.
What is the source or expression system of FGF 2 Protein?
Escherichia Coli.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.
What is the amino acid sequence of FGF 2 Protein?
AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 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 :
CARD18 HumanDescription:
Caspase Recruitment Domain Family, Member 18 Human Recombinant
Caspase recruitment domain family member 18, ICEBERG, pseudo-ICE, UNQ5804, Caspase-1 inhibitor Iceberg, ICEBERG caspase-1 inhibitor.
Product # :
PRO-1061Price :
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Shipped with Ice Packs
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Description
CARD18 Human Recombinant produced in E. coli is a single polypeptide chain containing 110 amino acids (1-90) and having a molecular mass of 12.3kDa.CARD18 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The LSM3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CARD18 belongs to the death-domain-fold superfamily which is induced by proinflammatory stimuli. CARD18 contains basically only a Caspase recruitment domain, inhibits generation of IL-1b by cooperating with caspase-1 and inhibiting connotation with RIP 2. The connotation of CARD18 to caspase-1 is enabled by the charge-charge interactions between the prodomain of caspase-1 and the surface charge of CARD18.
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Synonyms
Caspase recruitment domain family member 18, ICEBERG, pseudo-ICE, UNQ5804, Caspase-1 inhibitor Iceberg, ICEBERG caspase-1 inhibitor.
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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 MADQLLRKKR RIFIHSVGAG TINALLDCLL EDEVISQEDM NKVRDENDTV MDKARVLIDL VTGKGPKSCC KFIKHLCEED PQLASKMGLH
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 :
GM-CSF RatDescription:
Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Product # :
CYT-395Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF Rat was lyophilized with no additives.
Purity
Greater than 96.0% as determined by:
(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.
Citations
More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
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Background
What is the molecular weight/Mw of GM-CSF RAT Protein?
GM-CSF RAT Protein has a total Mw of 14.59kDa.
What is the source or expression system of GM-CSF RAT Protein?
Escherichia Coli.
What is the Purity of GM-CSF RAT Protein?
GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF RAT Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.
What is the amino acid sequence of GM-CSF RAT Protein?
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
What applications can GM-CSF RAT Protein be used in?
GM-CSF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF RAT Protein?
The endotoxin level is minimal, GM-CSF 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 :
HMGA1 HumanDescription:
High Mobility Group AT-Hook 1 Human Recombinant
High mobility group protein HMG-I/HMG-Y, HMG-I(Y), High mobility group AT-hook protein 1, High mobility group protein A1, High mobility group protein R , HMGA1, HMGIY, HMG-R, HMGA1A.
Product # :
PRO-887Price :
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Shipped with Ice Packs
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Description
HMGA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-107 a.a.) and having a molecular mass of 12.7kDa (Molecular weight on SDS-PAGE will appear higher).HMGA1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGA1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
High mobility group protein HMG-I/HMG-Y (HMGA1) belongs to the non-histone chromosomal high mobility group protein (HMG) family. HMGA1 is composed of a highly conserved AT-hook DNA-binding domain which mediates binding to AT-rich sequences in the minor groove of chromosomal DNA. HMGA1 functions as an architectural chromatin-binding transcription factor modifying the conformation of DNA by modulating nuclear protein-DNA complexes. Furthermore, HMGA1 is involved in numerous cellular processes including growth regulation, viral induction of beta-IFN gene and regulation of inducible gene transcription.
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Synonyms
High mobility group protein HMG-I/HMG-Y, HMG-I(Y), High mobility group AT-hook protein 1, High mobility group protein A1, High mobility group protein R , HMGA1, HMGIY, HMG-R, HMGA1A.
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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
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQLEH 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 :
CA1 Human, ActiveDescription:
Carbonic Anhydrase-1 Human Recombinant, BioActive
CA1, CA-I, CAB.
Product # :
ENZ-1137Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa. CA1 Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CA1 Human protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 at 37C.
Citations
More Info
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Introduction
CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.
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Synonyms
CA1, CA-I, CAB.
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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 MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.
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 :
CRKL HumanDescription:
V-crk Sarcoma Virus CT10 Oncogene Homolog (Avian)-Like Human Recombinant
Crk-like protein, CRKL.
Product # :
PRO-063Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRKL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (1-303 a.a.) and having a molecular mass of 35.9kDa (Molecular size on SDS-PAGE will appear higher). The CRKL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRKL solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.
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Synonyms
Crk-like protein, CRKL.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRDSSTCPGDYVL SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE.
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 :
CCL18 HumanDescription:
Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Product # :
CHM-322Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
-
Introduction
Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-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 MIP-4 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
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
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Background
What is the molecular weight/Mw of CCL18 HUMAN Protein?
CCL18 HUMAN Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL18 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL18 HUMAN Protein?
CCL18 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL18 HUMAN Protein?
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL18 HUMAN Protein?
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
What applications can CCL18 HUMAN Protein be used in?
CCL18 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL18 HUMAN Protein?
The endotoxin level is minimal, CCL18 HUMAN Protein was purified using conventional chromatography techniques.Who supplies recombinant CCL18 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL18 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
BAIAP2 HumanDescription:
BAI1-Associated Protein 2 Human Recombinant
Brain-specific angiogenesis inhibitor 1-associated protein 2, BAI1-associated protein 2, Protein BAP2, Fas ligand-associated factor 3, FLAF3, IRS-58, IRSp53/58, IRSP53.
Product # :
PRO-1022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BAIAP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 530 amino acids (1-522) and having a molecular mass of 58.4kDa.BAIAP2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BAIAP2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BAIAP2 is a ubiquitous regulator of the actin cytoskeleton. Controled by the Rho-family GTPases BAIAP2 facilitates filopodia development. BAIAP2 is expressed in the cytoplasm and binds small membrane-bound G-proteins to cytoplasmic effector proteins. BAIAP2 was identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is related to an autosomal dominant neurodegenerative disease.
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Synonyms
Brain-specific angiogenesis inhibitor 1-associated protein 2, BAI1-associated protein 2, Protein BAP2, Fas ligand-associated factor 3, FLAF3, IRS-58, IRSp53/58, IRSP53.
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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
MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPSKIPERA VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN GVTGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTAENK TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLAIPPP DYGAASRAFP AQTASGFKQR PYSVAVPAFS QGLDDYGARS MSSGSGTLVS TVVEHHHHHH
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 HumanDescription:
Biglycan Human Recombinant
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
Product # :
PRO-1382Price :
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Description
BGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (38-368a.a) and having a molecular mass of 39.5kDa. BGN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
BGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
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
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
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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 MDEEASGADT SGVLDPDSVT PTYSAMCPFG CHCHLRVVQC SDLGLKSVPK EISPDTTLLD LQNNDISELR KDDFKGLQHL YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK GVFSGLRNMN CIEMGGNPLE NSGFEPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLARVPSGL PDLKLLQVVY LHSNNITKVG VNDFCPMGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT DRLAIQFGNY KK.
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 :
STAMBP HumanDescription:
STAM Binding Protein Human Recombinant
STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.
Product # :
PRO-017Price :
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Shipped with Ice Packs
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Description
STAMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424) and having a molecular mass of 50kDa. STAMBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STAMBP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE..
Citations
More Info
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Introduction
STAM Binding Protein (STAMBP) is a zinc metalloprotease which specifically cleaves Lys-63-linked polyubiquitin chains, however it doesn’t cleave Lys-48-linked polyubiquitin chains. STAMBP has a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. In addition, STAMBP potentiates BMP signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. STAMBP also has a major role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is essential for efficient EGFR degradation but not for its internalization. STAMBP is also involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.
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Synonyms
STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSDHGDV SLPPEDRVRA LSQLGSAVEV NEDIPPRRYF RSGVEIIRMA SIYSEEGNIE HAFILYNKYI TLFIEKLPKH RDYKSAVIPE KKDTVKKLKE IAFPKAEELK AELLKRYTKE YTEYNEEKKK EAEELARNMA IQQELEKEKQ RVAQQKQQQL EQEQFHAFEE MIRNQELEKE RLKIVQEFGK VDPGLGGPLV PDLEKPSLDV FPTLTVSSIQ PSDCHTTVRP AKPPVVDRSL KPGALSNSES IPTIDGLRHV VVPGRLCPQF LQLASANTAR GVETCGILCG KLMRNEFTIT HVLIPKQSAG SDYCNTENEE ELFLIQDQQG LITLGWIHTH PTQTAFLSSV DLHTHCSYQM MLPESVAIVC SPKFQETGFF KLTDHGLEEI SSCRQKGFHP HSKDPPLFCS CSHVTVVDRA VTITDLR.
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 :
BRK1 HumanDescription:
BRK1 Human Recombinant
BRICK1 SCAR/WAVE Actin-Nucleating Complex Subunit, Haematopoietic Stem/Progenitor Cell Protein 300, Homolog (Arabidopsis Thaliana), Chromosome 3 Open Reading Frame 10, Probable Protein BRICK1, BRICK1, HSPC300, MDS027, C3orf10.
Product # :
PRO-1836Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BRK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (1-75) and having a molecular mass of 11.0 kDa. BRK1 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The BRK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BRK1 is a member of the BRK1 family. BRK1 takes part in regulating actin and microtubule organization and is a fragment of a WAVE complex which activates the Arp2/3 complex.
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Synonyms
BRICK1 SCAR/WAVE Actin-Nucleating Complex Subunit, Haematopoietic Stem/Progenitor Cell Protein 300, Homolog (Arabidopsis Thaliana), Chromosome 3 Open Reading Frame 10, Probable Protein BRICK1, BRICK1, HSPC300, MDS027, C3orf10.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGQEDP VQREIHQDWA NREYIEIITS SIKKIADFLN SFDMSCRSRL ATLNEKLTAL ERRIEYIEAR VTKGETLT
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 :
CCL6 RatDescription:
C-10 Rat Recombinant (CCL6)
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
Product # :
CHM-268Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
C-10 Rat Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 94 amino acids and having a total molecular mass of 10.4kDa. C-10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25 ug/ml.Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1. -
Synonyms
Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized C-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution C-10 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 reconstitute the lyophilized C-10 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
GLIQDTVKED RPFNPTIIHQ GFQDSSDCCF SYASQIPCSR FIYYFPTSGG CTKPGIIFVT RKRKRVCANP SDQRVQTCIS TLKLGPRSGN SAIA.
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Background
What is the molecular weight/Mw of CCL6 RAT Protein?
CCL6 RAT Protein has a total Mw of 10.4kDa.
What is the source or expression system of CCL6 RAT Protein?
Escherichia Coli.
What is the Purity of CCL6 RAT Protein?
CCL6 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL6 RAT Protein?
Determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25 ug/ml.
What is the amino acid sequence of CCL6 RAT Protein?
GLIQDTVKED RPFNPTIIHQ GFQDSSDCCF SYASQIPCSR FIYYFPTSGG CTKPGIIFVT RKRKRVCANP SDQRVQTCIS TLKLGPRSGN SAIA.
What applications can CCL6 RAT Protein be used in?
CCL6 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL6 RAT Protein?
The endotoxin level is minimal, CCL6 RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL6 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL6 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
KLK10 HumanDescription:
Kallikrein-10 Human Recombinant
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
Product # :
ENZ-795Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (34-276) and having a molecular mass of 29.1kDa.KLK10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLK10 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.
Citations
More Info
-
Introduction
Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.
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Synonyms
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSN.
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 :
CLNS1A HumanDescription:
Chloride Channel, Nucleotide-Sensitive, 1A Human Recombinant
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
Product # :
PRO-1277Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CLNS1A Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.8kDa (molecular size on SDS-PAGE will appear higher).CLNS1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CLNS1A solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Methylosome subunit pICln (CLNS1A), is a member of the pICln (TC 1.A.47) family. CLNS1A takes part in multiple regulatory pathways. CLNS1A interaction with Sm proteins, inhibits their compilation on U RNA and interferes with snRNP biogenesis. CLNS1A inhibits the binding of survival motor neuron protein (SMN) to Sm proteins. Methylosome subunit pICln is related with the plasma membrane where it functions as a chloride present regulator.
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Synonyms
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
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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 MGSHMSFLKS FPPPGPAEGL LRQQPDTEAV LNGKGLGTGT LYIAESRLSW LDGSGLGFSL EYPTISLHAL SRDRSDCLGE HLYVMVNAKF EEESKEPVAD EEEEDSDDDV EPITEFRFVP SDKSALEAMF TAMCECQALH PDPEDEDSDD YDGEEYDVEA HEQGQGDIPT FYTYEEGLSH LTAEGQATLE RLEGMLSQSV SSQYNMAGVR TEDSIRDYED GMEVDTTPTV AGQFEDADVD H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CD44 Human, HisDescription:
CD44, His Tag Human Recombinant
cd-44.
Product # :
PRO-2834Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The CD44Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CD44His-Tagged Fusion Protein, produced in E. coli, is a 28kDa protein containing 175 amino acid residues.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
cd-44.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized CD44 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
EETATQKEQWFGNRWHEGYRQTPREDSHSTTGTAAASAHTSHPMQG RTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSTTLQPTANP NTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRN DVTGGRRDPNHSEGSTTLLEGYTSHYPHTK
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Background
CD44 is a cell-surface glycoprotein which take part in migration, cell-cell interactions and cell adhesion. CD44 is a receptor of hyaluronic acid which interacts with other ligands such as collagens, osteopontin and matrix metalloproteinases. CD44 has various of functions such as lymphocyte activation, tumor metastasis, recirculation & homing and hematopoiesis.
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 :
UCN3 HumanDescription:
Urocortin 3 Human Recombinant
Stresscopin, urocortin-iii.
Product # :
HOR-056Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The UCN3Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCN3His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 161 amino acid residues of the UCN3Human, 1-161 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Stresscopin, urocortin-iii.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized UCN3at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Urocortin 3 also known as UCN3 is a part of the corticotropin-releasing factor (CRF) family of peptides, which are involved in metabolism, stress response and neuroendocrine regulation. UCN3 exerts its biological effects through interactions with CRFR2. UCN3 takes a main part in mediating few important biological processes, specially those associated with energy metabolism, stress response and the regulation of the hypothalamic-pituitary-adrenal (HPA) axis. UCN3 expressed mainly in the brain in areas such as the hypothalamus, as well as in peripheral tissues, including the heart and adipose tissue.
What is the molecular weight/Mw of UCN3 HUMAN Protein?
UCN3 HUMAN Protein has a total Mw of 20kDa.
What is the source or expression system of UCN3 HUMAN Protein?
Escherichia Coli.
What is the Purity of UCN3 HUMAN Protein?
UCN3 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of UCN3 HUMAN Protein?
The biological functionality of UCN3 HUMAN Protein will be determined in the future.
What applications can UCN3 HUMAN Protein be used in?
UCN3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for UCN3 HUMAN Protein?
The endotoxin level is minimal, UCN3 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.
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Name :
EledoisinDescription:
Eledoisin
Product # :
PRO-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Eledoisin’s molecular weight is 1188.4 having an amino acid sequence of Glp-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2 and a molecular formula of C54H85N13O15S.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Eledoisin is an undecapeptide formed in the venom gland of several species of octopuses and is used as a vasodilator and a contraction agent of extravascular smooth muscle.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eledoisin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Eledoisin 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 Eledoisin 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 :
DHODH HumanDescription:
Dihydroorotate Dehydrogenase Human Recombinant
Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.
Product # :
ENZ-642Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DHODH Human Recombinant produced in E. coli is a single polypeptide chain containing 390 amino acids (31-395) and having a molecular mass of 42.3 kDa.DHODH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DHODH solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Dihydroorotate dehydrogenase quinone (DHODH) is a member of the dihydroorotate dehydrogenase family. DHODH is a mitochondrial protein found on the outer surface of the inner mitochondrial membrane. DHODH catalyzes the 4th enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate (with quinone as electron acceptor), in de novo pyrimidine biosynthesis. DHODH gene defects cause the postaxial acrofacial dysostosis (POADS), also known as Miller syndrome.
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Synonyms
Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.
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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
GSSHHHHHH SSGLVPRGSH MGSHMTGDER FYAEHLMPTL QGLLDPESAH RLAVRFTSLG LLPRARFQDS DMLEVRVLGH KFRNPVGIAA GFDKHGEAVD GLYKMGFGFV EIGSVTPKPQ EGNPRPRVFR LPEDQAVINR YGFNSHGLSV VEHRLRARQQ KQAKLTEDGL PLGVNLGKNK TSVDAAEDYA EGVRVLGPLA DYLVVNVSSP NTAGLRSLQG KAELRRLLTK VLQERDGLRR VHRPAVLVKI APDLTSQDKE DIASVVKELG IDGLIVTNTT VSRPAGLQGA LRSETGGLSG KPLRDLSTQT IREMYALTQG RVPIIGVGGV SSGQDALEKI RAGASLVQLY TALTFWGPPV VGKVKRELEA LLKEQGFGGV TDAIGADHRR.
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 :
Activin-A Human Plant-ActiveDescription:
Activin-A Human Recombinant, Plant-Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-414Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana.
Formulation
Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4
Purity
Greater than 98% as obsereved by SDS-PAGE.
Biological Activity
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.Citations
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
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Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
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Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS. -
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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.