Search: 1000 results found for "phd finger protein"

Description:

Peptidase Inhibitor 16 Human Recombinant

Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

Product # :

ENZ-113

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Description

The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.

Source

HEK293 (Human Embryonic Kidney cell line).

Formulation

PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized PI16 Human recombinant 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.

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.

Description:

Secretagogin Rat Recombinant

SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

Product # :

PRO-657

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Description

Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas.
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
Physical Appearance
Sterile 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.
Solubility
Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

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.

Description:

Hepatoma Derived Growth Factor-Like 1 Human Recombinant

Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.

Product # :

CYT-850

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Description

HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.
Synonyms
Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.
Background
What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.

What is the source or expression system of HDGFL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of HDGFL1 HUMAN Protein?
HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of HDGFL1 HUMAN Protein?
The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of HDGFL1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

What applications can HDGFL1 HUMAN Protein be used in?
HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HDGFL1 HUMAN Protein?
The endotoxin level is minimal, HDGFL1 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.

Description:

C-Reactive Protein Human

C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

Product # :

PRO-557

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Description

Human CRP produced in Human plasma having a molecular mass of 114 kDa. It can be used as a marker for inflammation and also used for monitoring and prediction of future events in coronary artery disease.

Source

Human Plasma.

Formulation

The protein solution is in 20mM TRIS buffer pH 8.0 containing 0.28M NaCl, 0.09% NaN3 and 5mM CaCl2.

Purity

Greater than 96.0%.

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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically ( up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Physical Appearance
Sterile Filtered clear solution.
Stability
Human CRP should be stored at 2-8°C. Do not freeze!
Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG and HIV/HBV/HCV (PCR).

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.

Description:

Midkine Human Recombinant

NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

Product # :

CYT-192

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Description

Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated 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 neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.

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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.
Synonyms
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Midkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine 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
It is recommended to reconstitute the lyophilized Midkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.

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.

Description:

Processing Of Precursor 4 Human Recombinant

RPP29, Ribonuclease P protein subunit p29, hPOP4.

Product # :

PRO-1407

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Description

POP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a.) and having a molecular mass of 27.8kDa.POP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

POP4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Processing of Precursor 4 (POP4) is a member of the eukaryotic/archaeal RNase P protein component 1 family. POP4 is one of the protein subunits of the small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. POP4 is confined to the nucleus and associates promptly with the RNA component of this complexes.POP4 is participating in processing of precursor RNAs.
Synonyms
RPP29, Ribonuclease P protein subunit p29, hPOP4.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKSVIYH ALSQKEANDS DVQPSGAQRA EAFVRAFLKR STPRMSPQAR EDQLQRKAVV LEYFTRHKRK EKKKKAKGLS ARQRRELRLF DIKPEQQRYS LFLPLHELWK QYIRDLCSGL KPDTQPQMIQ AKLLKADLHG AIISVTKSKC PSYVGITGIL LQETKHIFKI ITKEDRLKVI PKLNCVFTVE TDGFISYIYG SKFQLRSSER SAKKFKAKGT IDL.

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.

Description:

Crystallin Alpha B Human Recombinant, His Tag

CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

Product # :

HSP-088

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Description

CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.
Background
Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.
Structural Insights into CRYAB Human Recombinant:
CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.
Cellular Functions in Proteostasis:
As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.
Implications in Neurodegenerative Disorders:
CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.
CRYAB in Cardiovascular Health:
The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.
Challenges and Future Directions:
While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.
CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.

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.

Description:

Phosphoglycerate Kinase 1 Human Recombinant, BioActive

Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.

Product # :

PKA-124

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Description

PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-417a.a.) and having a molecular mass of 46.8kDa.PGK1 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PGK1 solution (1mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 1mM DTT.

.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity: > 600unit/mg. One unit will convert 1 umole of 1,3-Bisphosphoglycerate to 3-PGA per minute at pH 8.0 at 37C.

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Introduction
Phosphoglycerate kinase 1, also referred to PGK1, is an X-linked enzyme whichfunctions in the glycolytic pathway.The gene encoding the erythrocyte enzyme PGK1 & it seems that PGK-1 plays a role as a polymerase alpha cofactor protein (primer recognition protein) as a glyxolytic enzyme role. The PGK1 catalyzes the reversible conversion of 1, 3-diphosphoglycerate to 3-phosphoglycerate during glycolysis, generating one molecule of ATP.
Synonyms
Phosphoglycerate kinase 1, MGC117307, MGC142128, MGC8947, MIG10, PGKA.
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 MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI

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Description:

Phosphofructokinase, Muscle Human Recombinant

EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.

Product # :

PKA-365

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Description

PFKM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 800 amino acids (1-780 a.a.) and having a molecular mass of 87.3 kDa. PFKM protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

PFKM Human solution containing 20mM Trsi HCl pH-8, 5mM DTT, 0.2M NaCl and 20% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.
Synonyms
EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD GGDHIKEATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAYNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITDEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIMEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK AMDEKKFDEA LKLRGRSFMN NWEVYKLLAH VRPPVSKSGS HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF QPVAELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI TRKRSGEAAV.

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.

Description:

Otoraplin Human Recombinant

Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.

Product # :

CYT-582

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Description

Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.
Synonyms
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR 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
It is recommended to reconstitute the lyophilized Otoraplin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
DIDFFCE.

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.

Description:

Myelin Basic Protein Human Recombinant

Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.

Product # :

PRO-1713

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Description

MBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197) and having a molecular mass of 23.9kDa.MBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.
Synonyms
Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGNHAGK RELNAEKAST NSETNRGESE KKRNLGELSR TTSEDNEVFG EADANQNNGT SSQDTAVTDS KRTADPKNAW QDAHPADPGS RPHLIRLFSR DAPGREDNTF KDRPSESDEL QTIQEDSAAT SESLDVMASQ KRPSQRHGSK YLATASTMDH ARHGFLPRHR DTGILDSIGR FFGGDRGAPK RGSGKVSSEE

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.

Description:

CXADR-Like Membrane Protein Human Recombinant

CXADR-Like Membrane Protein, CLMP, Adipocyte Adhesion Molecule, Coxsackie- And Adenovirus Receptor-Like Membrane Protein, ACAM, ASAM, Adipocyte-Specific Adhesion Molecule, CAR-Like Membrane Protein, CSBS, CSBM.

Product # :

PRO-1941

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Description

CLMP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (19-235) and having a molecular mass of 26.1 kDa.CLMP is fused to a 16 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CLMP 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.

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Introduction
The CTX family of proteins (including ASAM) are type I transmembrane proteins within the Ig superfamily, which localize to junctional complexes between endothelial and epithelial cells and may play a role in cell-cell adhesion. CLMP has a role in adipocyte differentiation and development of obesity. CLMP is required for normal small intestine development.
Synonyms
CXADR-Like Membrane Protein, CLMP, Adipocyte Adhesion Molecule, Coxsackie- And Adenovirus Receptor-Like Membrane Protein, ACAM, ASAM, Adipocyte-Specific Adhesion Molecule, CAR-Like Membrane Protein, CSBS, CSBM.
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.
Amino Acid Sequence
MASMTGGQQM GRGSHMTHTE IKRVAEEKVT LPCHHQLGLP EKDTLDIEWL LTDNEGNQKV VITYSSRHVY NNLTEEQKGR VAFASNFLAG DASLQIEPLK PSDEGRYTCK VKNSGRYVWS HVILKVLVRP SKPKCELEGE LTEGSDLTLQ CESSSGTEPI VYYWQRIREK EGEDERLPPK SRIDYNHPGR VLLQNLTMSY SGLYQCTAGN EAGKESCVVR VTVQYVQSIG MVA.

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.

Description:

Thyroid Stimulating Hormone Human Recombinant

Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

Product # :

HOR-050

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Description

Thyroid Stimulating Hormone Human Recombinant produced in HEK 293 cells.

Source

HEK 293 cells.

Formulation

Lyophilized from a concentrated 50mM ammonium bicarbonate.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The protein is biologically active using Siemens Centaur CP is standardized against WHO 3rd IS 81/565.

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Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Recombinant TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant TSH 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
It is recommended to reconstitute the lyophilized recombinant TSH in sterile 10 mM Sodium Phosphate, 150 mM Sodium Chloride, 1 mg/ml BSA, 0.1% Sodium Azide (optional), pH 7.4.
Background
Thyroid-stimulating hormone (TSH), also known as thyrotropin, is a glycoprotein hormone produced by the anterior pituitary gland. Its primary function is to regulate thyroid gland activity by stimulating the synthesis and secretion of thyroid hormones, thyroxine (T4) and triiodothyronine (T3). Recombinant human TSH (rhTSH) has emerged as a valuable tool in clinical practice, particularly in the management of thyroid disorders and in diagnostic procedures involving the thyroid gland. This paper aims to provide an overview of research on rhTSH, including its mechanism of action, activity, and therapeutic applications.
The mechanism of action of rhTSH involves binding to the TSH receptor (TSHR) on the surface of thyroid follicular cells. This interaction activates intracellular signalling pathways, including cyclic adenosine monophosphate (cAMP) production and protein kinase A (PKA) activation. These pathways stimulate various cellular processes within thyroid follicular cells, such as iodine uptake, thyroid hormone synthesis, and secretion.
What is the source or expression system of TSH PROTEIN Protein?
HEK 293 cells.

What is the Purity of TSH PROTEIN Protein?
TSH PROTEIN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of TSH PROTEIN Protein?
The protein is biologically active using Siemens Centaur CP is standardized against WHO 3rd IS 81/565.

What applications can TSH PROTEIN Protein be used in?
TSH PROTEIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TSH PROTEIN Protein?
The endotoxin level is minimal, TSH PROTEIN 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.

Description:

Bone Morphogenetic Protein-4 Human Recombinant

BMP4, ZYME, BMP2B, BMP2B1.

Product # :

CYT-361

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Description

Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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
It is recommended to reconstitute the lyophilized Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.

What is the source or expression system of BMP4 Protein?
Escherichia Coli.

What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.

What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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.

Description:

Recoverin Human Recombinant

RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin.

Product # :

PRO-441

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Description

Recoverin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids & having a molecular mass of 23kDa.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains 20mM Tris-HCl pH 8.0, 1mM EDTA, 2mM MgCl2 and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.
Synonyms
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin.
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
MGNSKSGALS KEILEELQLN TKFSEEELCS WYQSFLKDCP TGRITQQQFQ SIYAKFFPDT DPKAYAQHVF RSFDSNLDGT LDFKEYVIAL HMTTAGKTNQ KLEWAFSLYD VDGNGTISKNEVLEIVMAIF KMITPEDVKL LPDDENTPEK RAEKIWKYFG KNDDDKLTEK EFIEGTLANK EILRLIQFEP QKVKEKMKNA.

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.

Description:

Parkinson Disease Protein 7 Mouse Recombinant

Protein deglycase DJ-1, Parkinson disease protein 7 homolog.

Product # :

PRO-2226

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Description

PARK7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a) and having a molecular mass of 22.4kDa. PARK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PARK7 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).
Synonyms
Protein deglycase DJ-1, Parkinson disease protein 7 homolog.
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 MGSMASKRAL VILAKGAEEM ETVIPVDVMR RAGIKVTVAG LAGKDPVQCS RDVMICPDTS LEDAKTQGPY DVVVLPGGNL GAQNLSESPM VKEILKEQES RKGLIAAICA GPTALLAHEV GFGCKVTTHP LAKDKMMNGS HYSYSESRVE KDGLILTSRG PGTSFEFALA IVEALVGKDM ANQVKAPLVL KD.

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.

Description:

Insulin-Like Growth Factor Binding Protein-1 Human Recombinant

IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.

Product # :

CYT-299

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Description

IGFBP-1 Human Recombinant (26-259 a.a.) produced in NS0 is a single, glycosylated, polypeptide chain containing 234 amino acids and having a molecular mass of 25kDa. The IGFBP1 is purified by proprietary chromatographic techniques.

Source

Mouse myeloma cell line, NS0.

Formulation

IGFBP-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

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Introduction
IGFBP1 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGFBP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-BP1 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
It is recommended to reconstitute the lyophilized IBP-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
Background
What is the molecular weight/Mw of IGFBP1 HUMAN Protein?
IGFBP1 HUMAN Protein has a total Mw of 25kDa.

What is the source or expression system of IGFBP1 HUMAN Protein?
Mouse myeloma cell line, NS0.

What is the Purity of IGFBP1 HUMAN Protein?
IGFBP1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IGFBP1 HUMAN Protein?
The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

What is the amino acid sequence of IGFBP1 HUMAN Protein?
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

What applications can IGFBP1 HUMAN Protein be used in?
IGFBP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGFBP1 HUMAN Protein?
The endotoxin level is minimal, IGFBP1 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.

Description:

Vascular Endothelial Growth Factor (121) Human Recombinant, HEK

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-116

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Description

Recombinant Human VEGF 121 amino acids, produced in HEK cells is a glycosylated 37kDa homodimer and 50kDa homotrimer.The VEGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

VEGF was lyophilized from a 0.2µm filtered solution containing 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of HUVEC cells (Human Umbilical Vein Endothelial Cells), the ED₅₀ is 3ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF 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
It is recommended to reconstitute the lyophilized VEGF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

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.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, His Tag

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

Product # :

CYT-477

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Description

GMCSF Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids fragment (18-144) and having a molecular mass of 18.98kDa with an amino-terminal hexahistidine tag. GM-CSF Human Recombinant His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Granulocyte Macrophage Colony Stimulating Factor-His is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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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. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
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. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein has a total Mw of 18.98kDa.

What is the source or expression system of GM-CSF HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF HUMAN, HIS Protein?
The biological functionality of GM-CSF HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein is composed from 127 amino acids.

What applications can GM-CSF HUMAN, HIS Protein be used in?
GM-CSF HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF HUMAN, HIS Protein?
The endotoxin level is minimal, GM-CSF HUMAN, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

V-crk Sarcoma Virus CT10 Oncogene Human Recombinant

Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

Product # :

PRO-275

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Description

CRK 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 224 amino acids (1-204 a.a.) and having a molecular mass of 25kDa. The CRK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRK solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.
Synonyms
Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL IGGR.

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.

Description:

S-phase Kinase-Associated Protein 1 Isoform A Human Recombinant

SKP-1, EMC19, MGC34403, OCP-II, OCP2, p19A, SKP1A, TCEB1L, S-phase kinase-associated protein 1, Cyclin-A/CDK2-associated protein p19, p19skp1, RNA polymerase II elongation factor-like protein, Organ of Corti protein 2, OCP-2, Organ of Corti protein II, Transcription elongation factor B, SIII, SKP1.

Product # :

PKA-356

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Description

Recombinant Human SKP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18kDa.SKP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SKP1 protein solution contains 20mM Tris-HCl, pH-8, 10% glycerol and 50mM NaCl.

Purity

Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
SKP1 is a F-box enzyme which functions as a substrate recognition component of the SCF ubiquitin ligase complex which controls the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 binds to proteins containing an F-box motif, such as cyclin F, S-phase kinase-associated protein 2, and other regulatory proteins involved in ubiquitin dependent proteolysis. SKP1 takes part in the control of beta-catenin levels and the activity of beta-catenin dependent TCF transcription factors. SKP1 serves as an adapter that links the F-box protein to CUL1 in the SCF complex.
Synonyms
SKP-1, EMC19, MGC34403, OCP-II, OCP2, p19A, SKP1A, TCEB1L, S-phase kinase-associated protein 1, Cyclin-A/CDK2-associated protein p19, p19skp1, RNA polymerase II elongation factor-like protein, Organ of Corti protein 2, OCP-2, Organ of Corti protein II, Transcription elongation factor B, SIII, SKP1.
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
MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVGSTQFCL.

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.

Description:

Superoxide Dismutase-2 Mouse Recombinant

Superoxide dismutase [Mn], Superoxide Dismutase-2, mitochondrial, Sod-2.

Product # :

PRO-2192

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Description

SOD2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (25-222 a.a) and having a molecular mass of 24.6kDa.SOD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SOD2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.
Synonyms
Superoxide dismutase [Mn], Superoxide Dismutase-2, mitochondrial, Sod-2.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKHSLPDL PYDYGALEPH INAQIMQLHH SKHHAAYVNN LNATEEKYHE ALAKGDVTTQ VALQPALKFN GGGHINHTIF WTNLSPKGGG EPKGELLEAI KRDFGSFEKF KEKLTAVSVG VQGSGWGWLG FNKEQGRLQI AACSNQDPLQ GTTGLIPLLG IDVWEHAYYL QYKNVRPDYL KAIWNVINWE NVTERYTACK 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.

Description:

Fibronectin Type III And Ankyrin Repeat Domains 1 Human Recombinant

Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.

Product # :

PRO-1768

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Description

FANK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a) and having a molecular mass of 40.7kDa.FANK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FANK1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
FANK1 was localized in the nuclei of identical cells in the seminiferous epithelium. Depending on its nuclear localization, a gene ontology analysis proposes that FANK1 has a DNA binding activity therefor operates as a transcription factor. The extremely controlled expression of FANK1, suggests that it takes part in regulating gene expression in the transition from the meiotic phase to the haploid phase throughout spermatogenesis.
Synonyms
Fibronectin Type 3 And Ankyrin Repeat Domains 1, 1700007B22Rik.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEPQKIM PPSKPHPPVV GKVTHHSIEL YWDLEKKAKR QGPQEQWFRF SIEEEDPKMH TYGIIYTGYA TKHVVEGLEP RTLYRFRLKV TSPSGECEYS PLVSVSTTRE PISSEHLHRA VSVNDEDLLV RILQGGRVKV DVPNKFGFTA LMVAAQKGYT RLVKILVSNG TDVNLKNGSG KDSLMLACYA GHLDVVKYLR RHGASWQARD LGGCTALHWA ADGGHCSVIE WMIKDGCEVD VVDTGSGWTP LMRVSAVSGN QRVASLLIDA GANVNVKDRN GKTPLMVAVL NNHEELVQLL LDKGADASVK NEFGKGVLEM ARVFDRQSVV SLLEERKKKQ RPKKSCVC

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.

Description:

Darbepoetin-Alpha Human Recombinant

Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

Product # :

CYT-1263

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Description

Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells(CHO).

Formulation

Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

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Introduction
Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.
Synonyms
NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Darbepoetin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Darbepoetin 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
It is recommended to reconstitute the lyophilized Darbepoetin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.
Background
What is the molecular weight/Mw of DARBEPOETIN Protein?
DARBEPOETIN Protein has a total Mw of 38.5kDa.

What is the source or expression system of DARBEPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).

What is the Purity of DARBEPOETIN Protein?
DARBEPOETIN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of DARBEPOETIN Protein?
The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

What is the amino acid sequence of DARBEPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

What applications can DARBEPOETIN Protein be used in?
DARBEPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DARBEPOETIN Protein?
The endotoxin level is minimal, DARBEPOETIN 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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