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821 results found for “Biglycan”
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Name :
BLyS Human, PlantDescription:
BAFF (BLyS) Human Recombinant, Plant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-054Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
*activity results may vary with PBMC donors.
ED50 ? 50ng/mlMore Info
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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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 BAFF 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
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 19kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
What is the amino acid sequence of BLYS Protein?
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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 :
WIBG HumanDescription:
within BCGN Homolog Human Recombinant
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
Product # :
PRO-864Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
WIBG Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-204 a.a.) and having a molecular mass of 23.7 kDa. The WIBG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
WIBG Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.
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Synonyms
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
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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
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGLLEHHHH HH.
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 :
HPCAL1 HumanDescription:
Hippocalcin-Like 1 Human Recombinant
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3
Product # :
PRO-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.
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Synonyms
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
VILIP-3 -
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 MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF
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 :
BIRC5 HumanDescription:
Baculoviral IAP Repeat-Containing 5 Human Recombinant
BIRC-5, Baculoviral IAP repeat-containing protein 5, API4, EPR-1, Apoptosis inhibitor survivin, Apoptosis inhibitor 4, BIRC5, IAP4, Survivin.
Product # :
PRO-613Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Survivin Human Recombinant fused to a 152 a.a. N-terminal CaM-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-142 a.a.) and having a molecular mass of 33 kDa.
Source
Escherichia Coli.
Formulation
The BIRC5 solution contains 20mM Tris-HCl pH-7.5 & 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Survivin is part of the of the inhibitor of apoptosis (IAP) family, which encodes negative regulatory proteins that prevent apoptotic cell death. Members of the IAP family include multiple baculovirus IAP repeat (BIR) domains, but Survivin has only a single BIR domain.
Survivin is an inhibitor of caspase activation therefore leading to negative regulation of apoptosis. BIRC5 is expressed in Merkel cell carcinoma.
BIRC5 polymorphism causes survivin expression, thus contributing to the genetic susceptibility to lung cancer. BIRC5 expression in large cell lung cancer is substantially higher than in normal tissue cells. Survivin mRNA is up-regulated in tumors. Apoptotic response of infected intestinal epithelial cells is suppressed by C. parvum via upregulation of BIRC5, favoring parasite infection. Up-regulation of of Survivin is associated with breast carcinomas.
BIRC5 increases the activity of an oncolytic adenovirus in the presence of low-dose radiotherapy. ER- breast cancer cells become dependent on Notch-survivin signaling for their maintenance, in vivo. Survivin mRNA positive cases are related with bladder tumour recurrence elevated expression of survivin might play an important role of development in nasal polyps. -
Synonyms
BIRC-5, Baculoviral IAP repeat-containing protein 5, API4, EPR-1, Apoptosis inhibitor survivin, Apoptosis inhibitor 4, BIRC5, IAP4, Survivin.
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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
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAKG SHMGAPTLPP AWQPFLKDHR ISTFKNWPFL EGCACTPERM AEAGFIHCPT ENEPDLAQCF FCFKELEGWE PDDDPIEEHK KHSSGCAFLS VKKQFEELTL GEFLKLDRER AKNKIAKETN NKKKEFEETA KKVRRAIEQL AAMD.
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 :
DCTN2 (1-406) HumanDescription:
Dynactin 2 (1-406 a.a.) Human Recombinant
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
Product # :
PRO-1820Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (1-406 a.a) and having a molecular mass of 47.2kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
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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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAFA QELEELTSTS VEHIIVNPNA AYDKFKDKRV GTKGLDFSDR IGKTKRTGYE SGEYEMLGEG LGVKETPQQK YQRLLHEVQE LTTEVEKIKT TVKESATEEK LTPVLLAKQL AALKQQLVAS HLEKLLGPDA AINLTDPDGA LAKRLLLQLE ATKNSKGGSG GKTTGTPPDS SLVTYELHSR PEQDKFSQAA KVAELEKRLT ELETAVRCDQ DAQNPLSAGL QGACLMETVE LLQAKVSALD LAVLDQVEAR LQSVLGKVNE IAKHKASVED ADTQSKVHQL YETIQRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAN SLKDNTTLLT QVQTTMRENL ATVEGNFASI DERMKKLGK.
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 :
BIRC7 Human, (1-280 a.a.)Description:
Baculoviral IAP Repeat-Containing 7 (1-280 a.a.) Human Recombinant
Baculoviral IAP repeat-containing protein 7, KIAP, MLIAP, RNF50, ML-IAP, LIVIN, Kidney inhibitor of apoptosis protein, Melanoma inhibitor of apoptosis protein, RING finger protein 50, BIRC7.
Product # :
PRO-1042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BIRC7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-280 a.a.) and having a molecular mass of 33.4kDa.BIRC7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BIRC7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol, 300mM NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
BIRC7 is a part of the inhibitor of apoptosis protein (IAP) family and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is necessary for inhibitory activity & cooperates with caspases, while the RING finger domain sometimes increases anti-apoptotic activity but doesn’t inhibit apoptosis by itself. 2 transcript variants encoding diverse isoforms have been found for this gene. The 2 isoforms have dissimilar antiapoptotic characteristics, with isoform a protecting cells from apoptosis induced by staurosporine and isoform b defending cells from apoptosis induced by etoposide.
BIRC7 has direct contact with several caspases together with caspase-3, caspase-7, & caspase –9. BIRC7 inhibits the activation of caspase-9 induced by Apaf-1, cytochrome c, and dATP. -
Synonyms
Baculoviral IAP repeat-containing protein 7, KIAP, MLIAP, RNF50, ML-IAP, LIVIN, Kidney inhibitor of apoptosis protein, Melanoma inhibitor of apoptosis protein, RING finger protein 50, BIRC7.
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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 MGSHMGPKDS AKCLHRGPQP SHWAAGDGPT QERCGPRSLG SPVLGLDTCR AWDHVDGQIL GQLRPLTEEE EEEGAGATLS RGPAFPGMGS EELRLASFYD WPLTAEVPPE LLAAAGFFHT GHQDKVRCFF CYGGLQSWKR GDDPWTEHAK WFPSCQFLLR SKGRDFVHSV QETHSQLLGS WDPWEEPEDA APVAPSVPAS GYPELPTPRR EVQSESAQEP GARDVEAQLR RLQEERTCKV CLDRAVSIVF VPCGHLVCAE CAPGLQLCPI CRAPVRSRVR TFLS.
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 :
SDC2 HumanDescription:
Syndecan-2 Human Recombinant
Syndecan 2, Heparan Sulfate Proteoglycan 1 Cell Surface-Associated, Heparan Sulfate Proteoglycan Core Protein, Syndecan Proteoglycan 2, Fibroglycan, HSPG1, SYND2, HSPG, Cell Surface-Associated Heparan Sulfate Proteoglycan 1, CD362 Antigen, Syndecan-2, CD362, SDC2.
Product # :
PRO-2449Price :
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Shipped with Ice Packs
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Description
SDC2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 135 amino acids (19-144a.a.) and having a molecular mass of 15kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDC2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SDC2 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
Syndecan 2 (SDC2) is a conserved family of heparan- and chondroitin-sulfate carrying transmembrane protein. Syndecan 2 is a cell membrane proteoglycan which modulates the activity and dynamics of some growth factor receptors and integrins. SDC2 is expressed in HSCs (hepatic stellate cells), a key cell type involved in matrix deposition in liver fibrotic disorders. SDC2 is implicated in the formation of specialized membrane domains and serves as a direct link between the extracellular environment and the organization of the cortical cytoplasm.
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Synonyms
Syndecan 2, Heparan Sulfate Proteoglycan 1 Cell Surface-Associated, Heparan Sulfate Proteoglycan Core Protein, Syndecan Proteoglycan 2, Fibroglycan, HSPG1, SYND2, HSPG, Cell Surface-Associated Heparan Sulfate Proteoglycan 1, CD362 Antigen, Syndecan-2, CD362, SDC2.
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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
ADPESRAELT SDKDMYLDNS SIEEASGVYP IDDDDYASAS GSGADEDVES PELTTSRPLP KILLTSAAPK VETTTLNIQN KIPAQTKSPE ETDKEKVHLS DSERKMDPAE EDTNVYTEKH SDSLFKRTEH 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.
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Name :
Glucagon HumanDescription:
Glucagon Human Recombinant
GLP1, GLP2, GRPP.
Product # :
HOR-237Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton. The Glucagon is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of recombinant Glucagon was formulated with 100mg of lactose.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.More Info
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Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
GLP1, GLP2, GRPP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glucagon although stable at room temperature for 3 weeks, should be stored at 40C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
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Solubility
It is recommended to reconstitute the lyophilized Glucagon sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.
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Background
What is the molecular weight/Mw of GLUCAGON HUMAN Protein?
GLUCAGON HUMAN Protein has a total Mw of 3.48kDa.
What is the source or expression system of GLUCAGON HUMAN Protein?
Escherichia Coli.
What is the Purity of GLUCAGON HUMAN Protein?
GLUCAGON HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GLUCAGON HUMAN Protein?
The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.
What is the amino acid sequence of GLUCAGON HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.
What applications can GLUCAGON HUMAN Protein be used in?
GLUCAGON HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GLUCAGON HUMAN Protein?
The endotoxin level is minimal, GLUCAGON 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 :
IFNG MouseDescription:
IFN-Gamma Mouse Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-358Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs. -
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IFNG MOUSE Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE Protein?
IFNG MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
What applications can IFNG MOUSE Protein be used in?
IFNG MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG 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.
- View Data Sheet
Name :
DCTN2 (1-401) HumanDescription:
Dynactin 2 (1-401 a.a.) Human Recombinant
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
Product # :
PRO-1776Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (1-401 a.a) and having a molecular mass of 46.6kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEE LTSTSVEHII VNPNAAYDKF KDKRVGTKGL DFSDRIGKTK RTGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKTTVKES ATEEKLTPVL LAKQLAALKQ QLVASHLEKL LGPDAAINLT DPDGALAKRL LLQLEATKNS KGGSGGKTTG TPPDSSLVTY ELHSRPEQDK FSQAAKVAEL EKRLTELETA VRCDQDAQNP LSAGLQGACL METVELLQAK VSALDLAVLD QVEARLQSVL GKVNEIAKHK ASVEDADTQS KVHQLYETIQ RWSPIASTLP ELVQRLVTIK QLHEQAMQFG QLLTHLDTTQ QMIANSLKDN TTLLTQVQTT MRENLATVEG NFASIDERMK KLGK.
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 :
MYBPC3 HumanDescription:
Myosin Binding Protein C, Cardiac Human Recombinant
Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.
Product # :
PRO-2292Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MYBPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Phe271) containing 281 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 29.6kDa.
Source
Escherichia Coli.
Formulation
MYBPC3 was filtered (0.4µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Myosin Binding Protein C, Cardiac (MYBPC3) is the cardiac isoform of myosin-binding protein C expressed exclusively in heart muscle. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase upon adrenergic stimulation may be associated with modulation of cardiac contraction. MYBPC3 gene mutations are one of the causes of familial hypertrophic cardiomyopathy. In vitro MYBPC3 binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. MYBPC3 may modulate muscle contraction or it may have a more structural role.
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Synonyms
Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
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. MYBPC3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHASMPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA 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 :
DCTN2 (1-403) HumanDescription:
Dynactin 2 (1-403 a.a.) Human Recombinant
Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.
Product # :
PRO-2303Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403 a.a) and having a molecular mass of 46.9kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
Dynactin 2 (P50), 50 KDa Dynein-Associated Polypeptide, Dynactin Complex 50 KDa Subunit, P50 Dynamitin, DCTN50, 50 KD Dynein-Associated Polypeptide, Epididymis Secretory Protein Li 77, Dynactin Complex 50 KD Subunit, DYNAMITIN, HEL-S-77, DCTN-50, RBP50.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEL EELTSTSVEH IIVNPNAAYD KFKDKRVGTK GLDFSDRIGK TKRTGYESGE YEMLGEGLGV KETPQQKYQR LLHEVQELTT EVEKIKTTVK ESATEEKLTP VLLAKQLAAL KQQLVASHLE KLLGPDAAIN LTDPDGALAK RLLLQLEATK NSKGGSGGKT TGTPPDSSLV TYELHSRPEQ DKFSQAAKVA ELEKRLTELE TAVRCDQDAQ NPLSAGLQGA CLMETVELLQ AKVSALDLAV LDQVEARLQS VLGKVNEIAK HKASVEDADT QSKVHQLYET IQRWSPIAST LPELVQRLVT IKQLHEQAMQ FGQLLTHLDT TQQMIANSLK DNTTLLTQVQ TTMRENLATV EGNFASIDER MKKLGK
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 :
SHH HumanDescription:
Sonic HedgeHog Human Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-676Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from 10mM Na3PO4, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.
More Info
-
Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized SHH in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP
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 :
CCN1 (275-381)Description:
Cysteine-Rich Angiogenic Inducer 61 (275-381 a.a.) Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-1235Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
The CYR61Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CYR61His-Tagged Fusion Protein, produced in E. coli, is a 17kDa protein containing 107 amino acid residues of the CYR61Human, 275-381 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.
More Info
-
Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized CYR61at -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.
-
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.
-
Background
Cysteine-Rich Angiogenic Inducer 61 also known as CYR61 is a growth factor-inducible, immediate-early gene which has many activities in various cancers. CYR61 is a part of to the CCN family a group of secreted extracellular matrix-associated proteins which regulate diverse biological processes including cell adhesion, proliferation, migration, survival and angiogenesis. CYR61 plays a significant role in development, tissue repair, wound healing, and various pathological conditions such as cancer and fibrosis. CYR61 is encoded by a growth factor-inducible immediate-early gene. CYR61 promotes the adhesion of endothelial cells by interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 17kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The biological functionality of CCN1 Protein will be determined in the future.
What is the amino acid sequence of CCN1 Protein?
CCN1 Protein is composed from 107 amino acids.
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 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 :
BAG3 HumanDescription:
BCL2-Associated Athanogene 3 Human Recombinant
BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.
Product # :
PRO-760Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BAG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 595 amino acids (1-575 a.a.) and having a molecular mass of 63.7 kDa. The BAG3 protein is fused to a 20 amino acid His Tag at N-terminus and purified by standard chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The BAG3 protein contains 20mM Tris buffer pH-8, 1mM EDTA, 10% glycerol and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
BAG3 Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG3 has anti-apoptotic activity. BAG proteins participate with Hip for their binding to Hsc70/Hsp70 ATPase domain and encourage substrate release. BAG proteins have about 45 amino acid BAG domain close to the C terminus however they differ noticeably in their N-terminal regions. BAG3 includes a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact particularly with the Hsc70 ATPase domain in vitro and in mammalian cells. They bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. BAG3 plays a role as a protein-refolding cochaperone of the bcl2 binding protein BAG family and as upregulated in response to persistent stress of cellular calcium balance dysregulation. BAG3 has been shown to diminish stress-induced apoptosis.
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Synonyms
BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.
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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 MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP.
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 :
Bcl XL Human, GSTDescription:
B-Cell Lymphoma Extra Large Human Recombinant, GST
BclXL, Bcl-X(L), Bcl-XL.
Product # :
PRO-640Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
Bcl-XL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-210.The Bcl-XL is expressed as GST-Tag fusion protein and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 10mM Tris-HCL pH-8, 1mM EDTA and 250mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein. -
Synonyms
BclXL, Bcl-X(L), Bcl-XL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Bcl-XL although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-XL 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.
-
Solubility
Suspend BclXL in 100?l of 0.5M Acetic acid, over night at 4°C.
Dilute 10 fold into selected buffer system.
Bcl-XL has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.
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 :
CD68 Human, 38kDaDescription:
CD68 Human Recombinant, 38kDa
Macrosialin, Gp110, CD68 antigen, CD68, SCARD1, DKFZp686M18236.
Product # :
PRO-293Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
CD68 Human Recombinant full length expressed in E.coli, shows a 38 kDa band on SDS-PAGE.CD68 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CD68 at 100µg/1ml in 50mM Tris-Acetate, pH7.5, 1mM EDTA, 20% Glycerol.
More Info
-
Introduction
CD68 encodes a 110-kD transmembrane glycoprotein that is highly expressed by human monocytes and tissue macrophages. It is a member of the lysosomal/endosomal-associated membrane glycoprotein (LAMP) family. The protein primarily localizes to lysosomes and endosomes with a smaller fraction circulating to the cell surface. It is a type I integral membrane protein with a heavily glycosylated extracellular domain and binds to tissue- and organ-specific lectins or selectins. The protein is also a member of the scavenger receptor family. Scavenger receptors typically function to clear cellular debris, promote phagocytosis, and mediate the recruitment and activation of macrophages. Alternative splicing results in multiple transcripts encoding different isoforms.
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Synonyms
Macrosialin, Gp110, CD68 antigen, CD68, SCARD1, DKFZp686M18236.
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Physical Appearance
Sterile Filtered clear solution.
-
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.
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 :
SPARC MouseDescription:
Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine
Product # :
PRO-2658Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPARC Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (18-302a.a) and having a molecular mass of 33.3kDa.SPARC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SPARC solution (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Secreted Protein Acidic & Rich in Cysteine (SPARC) protein is coded by the SPARC gene in humans. SPARC is a glycoprotein located in bones that binds to calcium. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, mainly in areas of tissue morphogenesis and remodelling. Asides from calcium, SPARC can also bind to collagen.
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Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine
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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
APQQTEVAEE IVEEETVVEE TGVPVGANPV QVEMGEFEDG AEETVEEVVA DNPCQNHHCK HGKVCELDES NTPMCVCQDP TSCPAPIGEF EKVCSNDNKT FDSSCHFFAT KCTLEGTKKG HKLHLDYIGP CKYIAPCLDS ELTEFPLRMR DWLKNVLVTL YERDEGNNLL TEKQKLRVKK IHENEKRLEA GDHPVELLAR DFEKNYNMYI FPVHWQFGQL DQHPIDGYLS HTELAPLRAP LIPMEHCTTR FFETCDLDND KYIALEEWAG CFGIKEQDIN KDLVIHHHHH 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.
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Name :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
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Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CLIC1 HumanDescription:
Chloride Intracellular Channel 1 Human Recombinant
ACBP, ACBD1, CCK-RP, EP, CLIC1, G6, NCC27, Nuclear chloride ion channel 27, Chloride channel ABP, Regulatory nuclear chloride ion channel protein, hRNCC, Chloride intracellular channel protein 1.
Product # :
PRO-833Price :
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Description
CLIC1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261amino acids (1-241a.a.) and having a molecular mass of 29 kDa. CLIC1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CLIC1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Chloride channels are various group of proteins that control fundamental cellular processes including stabilization of cell membrane potential, transepithelial transport, regulation of intracellular pH, and maintenance of cell volume. CLIC1 is part of the p64 family and is localized to the cell nucleus. CLIC1 displays both nuclear and plasma membrane chloride ion channel activity. CLIC1 inserts into membranes and forms chloride ion channels. CLIC1 channel activity depends on the pH. CLIC1 membrane insertion is redox-regulated and happens under oxydizing conditions.
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Synonyms
ACBP, ACBD1, CCK-RP, EP, CLIC1, G6, NCC27, Nuclear chloride ion channel 27, Chloride channel ABP, Regulatory nuclear chloride ion channel protein, hRNCC, Chloride intracellular channel protein 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 MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTAGLDI FAKFSAYIKN SNPALNDNLE KGLLKALKVL DNYLTSPLPE EVDETSAEDE GVSQRKFLDG NELTLADCNL LPKLHIVQVV CKKYRGFTIP EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVAKAL K.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GPC4 HumanDescription:
Glypican-4 Human Recombinant
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
Product # :
PRO-1912Price :
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Description
GPC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (401-529a.a) and having a molecular mass of 18kDa.GPC4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GPC4 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.
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Synonyms
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSSSLP SNVCNDERMA AGNGNEDDCW NGKGKSRYLF AVTGNGLANQ GNNPEVQVDT SKPDILILRQ IMALRVMTSK MKNAYNGNDV DFFDISDESS GEGSGSGCEY QQCPSEFDYN ATDHAGKSAN EKADS
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 :
HLA-DOB HumanDescription:
Major Histocompatibility Complex Class II DO Beta Human Recombinant
HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.
Product # :
PRO-1967Price :
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Description
HLA-DOB Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (27-224) and having a molecular mass of 25.2 kDa.HLA-DOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HLA-DOB solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Major Histocompatibility Complex Class II DO Beta (HLA-DOB) is a part of the HLA class II beta chain paralogues. This class II beta chain is a heterodimer which is located in intracellular vesicles and consists of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. HLA-DOB which interacts with the HLA-DM molecule in B-cells is a significant modulator in the HLA class II restricted antigen presentation pathway. Class II molecules are expressed in antigen presenting cells such as B lymphocytes, dendritic cells and macrophages.
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Synonyms
HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.
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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 MGSGTDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSRQAVD GVCRHNYRLG APFTVGRKVQ PEVTVYPERT PLLHQHNLLH CSVTGFYPGD IKIKWFLNGQ EERAGVMSTG PIRNGDWTFQ TVVMLEMTPE LGHVYTCLVD HSSLLSPVSV EWRAQSEYSW RK.
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 :
EMCN HumanDescription:
Endomucin Human Recombinant
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
Product # :
PRO-1156Price :
Quantity :
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Description
EMCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (19-190 a.a) and having a molecular mass of 20.5kDa.EMCN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EMCN protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Endothelial sialomucin (Endomucin) interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix. Endomucin is expressed in the heart, kidney and lung.
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Synonyms
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
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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 MGSHMNSTGV LEAANNSLVV TTTKPSITTP NTESLQKNVV TPTTGTTPKG TITNELLKMS LMSTATFLTS KDEGLKATTT DVRKNDSIIS NVTVTSVTLP NAVSTLQSSK PKTETQSSIK TTEIPGSVLQ PDASPSKTGT LTSIPVTIPE NTSQSQVIGT EGGKNASTSA TSRSYSS.
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 :
HAPLN1 Human, HEKDescription:
Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant, HEK
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
Product # :
PRO-2776Price :
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Description
HAPLN1 Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 345 amino acids (16-354 a.a.) and having a molecular mass of 39.3kDa. HAPLN1 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
HAPLN1 protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤ 1 ug/ml and is measured by its binding ability in a functional ELISA with Hyaluronic acid.
More Info
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Synonyms
Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.
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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
DHLSDNYTLD HDRAIHIQAE NGPHLLVEAE QAKVFSHRGG NVTLPCKFYR DPTAFGSGIH KIRIKWTKLT SDYLKEVDVF VSMGYHKKTY GGYQGRVFLK GGSDSDASLV ITDLTLEDYG RYKCEVIEGL EDDTVVVALD LQGVVFPYFP RLGRYNLNFH EAQQACLDQD AVIASFDQLY DAWRGGLDWC NAGWLSDGSV QYPITKPREP CGGQNTVPGV RNYGFWDKDK SRYDVFCFTS NFNGRFYYLI HPTKLTYDEA VQACLNDGAQ IAKVGQIFAA WKILGYDRCD AGWLADGSVR YPISRPRRRC SPTEAAVRFV GFPDKKHKLY GVYCFRAYNH HHHHH.
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Background
Bibliography:
Armingol, E., Officer, A., Harismendy, O., & Lewis, N. E. (2020). Deciphering cell-cell interactions and communication from gene expression. Nature Reviews Genetics, 21(2), 71-88.
Bonnans, C., Chou, J., & Werb, Z. (2014). Remodelling the extracellular matrix in development and disease. Nature Reviews Molecular Cell Biology, 15(12), 786-801.
Bönnemann, C. G. (2011). The collagen VI-related myopathies: muscle meets its matrix. Nature Reviews Neurology, 7(7), 379-390.
Choi, H., Lee, R. H., Bazhanov, N., Oh, J. Y., & Prockop, D. J. (2011). Anti-inflammatory protein TSG-6 secreted by activated MSCs attenuates zymosan-induced mouse peritonitis by decreasing TLR2/NF-κB signaling in resident macrophages. Blood, 118(2), 330-338.
Lesley, J., Hyman, R., & Kincade, P. W. (1993). CD44 and its interaction with extracellularmatrix. Advances in Immunology, 54, 271-335.
Sherman, L. S., Rizvi, T. A., Karyala, S., & Ratner, N. (2000). CD44 enhances neuregulin signaling by Schwann cells. The Journal of Cell Biology, 150(5), 1071-1084.
Toole, B. P. (2004). Hyaluronan: from extracellular glue to pericellular cue. Nature Reviews Cancer, 4(7), 528-539.
Yamada, Y., Itano, N., Narimatsu, H., Kudo, T., Morozumi, K., Hirohashi, S., ... & Kimata, K. (2004). Elevated transcript level of hyaluronan synthase1 gene correlates with poor prognosis of human colon cancer. Clinical & Experimental Metastasis, 21(1), 57-63.
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.