Difference between revisions of "Part:BBa K1898300"

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<partinfo>BBa_K1898300 short</partinfo>
 
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This gene codes for CRYAA, or crystallin alpha A, a crystallin protein that is more restricted to the lens.  
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This gene codes for CRYAA, also known as crystallin alpha A, a crystallin protein that is more restricted to the lens.  
  
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===Usage and Biology===
 
===Usage and Biology===
 
Alpha crystallin is the most abundant protein in the lens. Out of the two types of alpha crystallin proteins, alpha A is more restricted to the lens and has a 3:1 ratio to alpha B [1]. It has been found that crystallin alpha A has chaperone activity to maintain normal protein interaction [2].  
 
Alpha crystallin is the most abundant protein in the lens. Out of the two types of alpha crystallin proteins, alpha A is more restricted to the lens and has a 3:1 ratio to alpha B [1]. It has been found that crystallin alpha A has chaperone activity to maintain normal protein interaction [2].  
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[1]Genes and mapped phenotypes. (n.d.). from https://www.ncbi.nlm.nih.gov/gene/1410
 
[1]Genes and mapped phenotypes. (n.d.). from https://www.ncbi.nlm.nih.gov/gene/1410
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[2]Usha, A. P. (n.d.). Crystallins in the eye: Function and pathology. from http://www.sciencedirect.com/science/article/pii/S1350946206000553
 
[2]Usha, A. P. (n.d.). Crystallins in the eye: Function and pathology. from http://www.sciencedirect.com/science/article/pii/S1350946206000553
  
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<partinfo>BBa_K1898300 parameters</partinfo>
 
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==Gel Pictures==
 
==Gel Pictures==

Latest revision as of 18:18, 18 October 2016


CRYAA, crystallin alpha A

This gene codes for CRYAA, also known as crystallin alpha A, a crystallin protein that is more restricted to the lens.

Usage and Biology

Alpha crystallin is the most abundant protein in the lens. Out of the two types of alpha crystallin proteins, alpha A is more restricted to the lens and has a 3:1 ratio to alpha B [1]. It has been found that crystallin alpha A has chaperone activity to maintain normal protein interaction [2].

In our project, we made CRYAA because we wanted to monitor crystallin protein's response to oxidative stress and to test our prevention and treatment for cataracts.

[1]Genes and mapped phenotypes. (n.d.). from https://www.ncbi.nlm.nih.gov/gene/1410

[2]Usha, A. P. (n.d.). Crystallins in the eye: Function and pathology. from http://www.sciencedirect.com/science/article/pii/S1350946206000553


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 59
  • 1000
    COMPATIBLE WITH RFC[1000]


Gel Pictures

We digested CRYAA with Xbal and Pst1 enzymes. The expected band size is ~700 bp. In the gel picture shown below, lane 1 is 1kb ladder and bands with the expected size are boxed in red:

Cryaa_pcr_gel_check.png

Sequencing

CRYAA DNA was sent to sequencing after it's moved into an iGEM backbone. The sequencing result confirms that CRYAA is right.

  • The four enzyme cutting sites are highlighted in red
  • CRYAA is highlighted in light blue

Cryaa.png